Welcome to LookChem.com Sign In|Join Free

CAS

  • or

147-85-3

Post Buying Request

147-85-3 Suppliers

Recommended suppliersmore

  • Product
  • FOB Price
  • Min.Order
  • Supply Ability
  • Supplier
  • Contact Supplier

147-85-3 Usage

Chemical Description

L-proline serves as the starting material, while the other chemicals are used for protection, activation, and functionalization of the intermediate compounds.

Physical properties

L-Proline, an amino acid, is odorless or has a slight, characteristic odor with a slightly sweet taste. It is synthesized from L-glutamine and L-glutamate via L-ornithine in intestine, and from L-ornithine in liver. It is widely used as an ingredient in infusion and infant formula.

Chemical Properties

Different sources of media describe the Chemical Properties of 147-85-3 differently. You can refer to the following data:
1. L-Proline is a colorless to white crystal or crystalline powder at room temperature, slightly odorous, slightly sweet in taste, easily soluble in water, insoluble in ethanol, insoluble in diethyl ether and n-butanol, yellow in case of hydrated ninhydrin test solution, glacial acetic acid Red after acidification; pH=6.3, decomposition point is 220-222°C; specific optical rotation [α]20D-85° (0.5-2.0mg/ml, H2O), [α]20D-60.4° (0.5-2.0mg /ml, 5mol/LHCl).
2. L-Proline, an amino acid, is colorless to white crystal or crystalline powder that has a slight, characteristic odor with a slightly sweet taste. It is soluble in water, insoluble in ethanol, diethyl ether and n-butanol, yellow in case of hydrated ninhydrin test solution, glacial acetic acid Red after acidification; pH=6.3, decomposition point is 220-222°C; specific optical rotation [α]20D-85° (0.5-2.0mg/ml, H2O), [α]20D-60.4° (0.5-2.0mg /ml, 5mol/LHCl). It is synthesized from L-glutamine and L-glutamate via L-ornithine in intestine, and from L-ornithine in liver. It is widely used as an ingredient in infusion and infant formula.

Occurrence

Reported found as a component in many proteins; also widely occurring as the free acid in natural products. A major constituent of collagen, the main fibrous protein found in bone, cartilage and other connective tissue.

Uses

Different sources of media describe the Uses of 147-85-3 differently. You can refer to the following data:
1. L-Proline is used as asymmetric catalysts in organic synthesis and asymmetric aldol cyclization. It is involved in the Michael addition of dimethyl malonate to alfa-beta-unsaturated aldehydes. It is a precursor of hydroxyproline in collagen. It is an active component of collagen and involved in the proper functioning of joints and tendons. It finds uses in pharmaceutical, biotechnological applications due to its osmoprotectant property. Further, it is used with ninhydrin in the chromatography.
2. L-Proline is an amino acid and precursor (with vitamin C) for collagen, the building block of the structure of tendons, ligaments, arteries, veins and muscles. It is important in wound healing.

Preparation

Synthesis of L-proline: Using glutamic acid as a raw material, it is esterified with absolute ethanol under the catalysis of sulfuric acid, and triethanolamine is added to free the aminosulfate to obtain glutamic acid-δ-ethyl ester. The glutamic acid-δ-ethyl ester is then reduced with a metal reducing agent potassium borohydride to obtain crude proline, which is finally separated and purified to obtain crude L-proline.

Definition

ChEBI: L-proline is pyrrolidine in which the pro-S hydrogen at position 2 is substituted by a carboxylic acid group. L-Proline is the only one of the twenty DNA-encoded amino acids which has a secondary amino group alpha to the carboxyl group. It is an essential component of collagen and is important for proper functioning of joints and tendons. It also helps maintain and strengthen heart muscles. It has a role as a micronutrient, a nutraceutical, an algal metabolite, a Saccharomyces cerevisiae metabolite, an Escherichia coli metabolite, a mouse metabolite and a member of compatible osmolytes. It is a glutamine family amino acid, a proteinogenic amino acid, a proline and a L-alpha-amino acid. It is a conjugate base of a L-prolinium. It is a conjugate acid of a L-prolinate. It is an enantiomer of a D-proline. It is a tautomer of a L-proline zwitterion.

benefits

L-proline is considered a non-essential amino acid as it can be synthesised from arginine via the urea cycle in liver, and from glutamine/glutamic acid in the intestinal epithelium. It has a number of beneficial properties including connective tissue strengthening, Stronger Connective Tissue, Decreased Risk Of Heart Disease, Maintenance Of Muscle Tissueand skin health.

General Description

Different sources of media describe the General Description of 147-85-3 differently. You can refer to the following data:
1. L-Proline is a non-essential amino acid. Peptides bond to proline, making it a useful building block for proteins. It can be used as a cell culture media component for the commercial biomanufacturing of therapeutic recombinant proteins and monoclonal antibodies.Pharmaceutical secondary standards for application in quality control, provide pharma laboratories and manufacturers with a convenient and cost-effective alternative to the preparation of in-house working standards.
2. L-Proline is a non-essential amino acid. Peptides bond to proline, making it a useful building block for proteins. It can be used as a cell culture media component for the commercial biomanufacturing of therapeutic recombinant proteins and monoclonal antibodies.

Flammability and Explosibility

Nonflammable

Biochem/physiol Actions

Proline is a cyclic, non-essential, hydrophobic amino acid. It is a proteinogenic amino acid which is crucial for primary metabolism. In peptide chains, proline residues confer structural constraints and enhance the susceptibility of proximal peptide bonds to protease activity.

Purification Methods

A likely impurity is hydroxyproline. Purify L-proline via its picrate which is crystallised twice from water, then decomposed with 40% H2SO4. The picric acid is extracted with diethyl ether, the H2SO4 in solution is precipitated with Ba(OH)2, and the filtrate is evaporated. The residue is crystallised from hot absolute EtOH [Mellan & Hoover J Am Chem Soc 73 3879 1951] or EtOH/Et2O. Its solubility in H2O is >100%. It sublimes at 182-187o/0.3mm with 99.4% recovery and unracemised [Gross & Gradsky J Am Chem Soc 77 1678 1955]. It is hygroscopic and is stored in a desiccator. [Greenstein & Winitz The Chemistry of the Amino Acids J. Wiley, Vol 3 pp 2178-2199 1961, Beilstein 22 III/IV 8, 22/1 V 31.]

Structure and conformation

L-proline, also known as L-pyrrolidine-2-carboxylic acid, is a neutral amino acid. Although proline is classified as an amino acid, it is strictly speaking an imino acid, since it contains an imino group (carbon-nitrogen double bond). Due to its cyclic pyrrolidine side chain it is classified as a nonpolar aliphatic amino acid.

Check Digit Verification of cas no

The CAS Registry Mumber 147-85-3 includes 6 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 3 digits, 1,4 and 7 respectively; the second part has 2 digits, 8 and 5 respectively.
Calculate Digit Verification of CAS Registry Number 147-85:
(5*1)+(4*4)+(3*7)+(2*8)+(1*5)=63
63 % 10 = 3
So 147-85-3 is a valid CAS Registry Number.
InChI:InChI=1/C5H9NO2/c7-5(8)4-2-1-3-6-4/h4,6H,1-3H2,(H,7,8)/t4-/m1/s1

147-85-3 Well-known Company Product Price

  • Brand
  • (Code)Product description
  • CAS number
  • Packaging
  • Price
  • Detail
  • TCI America

  • (P0481)  L-Proline  >99.0%(HPLC)(T)

  • 147-85-3

  • 25g

  • 141.00CNY

  • Detail
  • TCI America

  • (P0481)  L-Proline  >99.0%(HPLC)(T)

  • 147-85-3

  • 250g

  • 821.00CNY

  • Detail
  • Alfa Aesar

  • (A10199)  L-Proline, 99%   

  • 147-85-3

  • 25g

  • 206.0CNY

  • Detail
  • Alfa Aesar

  • (A10199)  L-Proline, 99%   

  • 147-85-3

  • 100g

  • 621.0CNY

  • Detail
  • Alfa Aesar

  • (A10199)  L-Proline, 99%   

  • 147-85-3

  • 500g

  • 2531.0CNY

  • Detail
  • Sigma-Aldrich

  • (PHR1332)    pharmaceutical secondary standard; traceable to USP and PhEur

  • 147-85-3

  • PHR1332-500MG

  • 500.06CNY

  • Detail
  • Sigma-Aldrich

  • (93693)  L-Proline  certified reference material, TraceCERT®

  • 147-85-3

  • 93693-100MG

  • 1,117.35CNY

  • Detail
  • Sigma-Aldrich

  • (P0380)  L-Proline  ReagentPlus®, ≥99% (HPLC)

  • 147-85-3

  • P0380-10MG

  • 221.13CNY

  • Detail
  • Sigma-Aldrich

  • (P0380)  L-Proline  ReagentPlus®, ≥99% (HPLC)

  • 147-85-3

  • P0380-100G

  • 872.82CNY

  • Detail
  • Sigma-Aldrich

  • (P0380)  L-Proline  ReagentPlus®, ≥99% (HPLC)

  • 147-85-3

  • P0380-1KG

  • 6,236.10CNY

  • Detail
  • Sigma-Aldrich

  • (P0380)  L-Proline  ReagentPlus®, ≥99% (HPLC)

  • 147-85-3

  • P0380-5KG

  • 28,232.10CNY

  • Detail
  • Vetec

  • (V900338)  L-Proline  Vetec reagent grade, ≥99%

  • 147-85-3

  • V900338-100G

  • 145.08CNY

  • Detail

147-85-3SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 12, 2017

Revision Date: Aug 12, 2017

1.Identification

1.1 GHS Product identifier

Product name L-proline

1.2 Other means of identification

Product number -
Other names QCR-1

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only. Food additives -> Flavoring Agents
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:147-85-3 SDS

147-85-3Synthetic route

(2S)-N-allyloxycarbonyl-L-proline
110637-44-0

(2S)-N-allyloxycarbonyl-L-proline

L-proline
147-85-3

L-proline

Conditions
ConditionsYield
With diethylamine; palladium diacetate; trisodium tris(3-sulfophenyl)phosphine In water; acetonitrile for 0.25h; Ambient temperature;100%
(S)-Pyrrolidine-2-carboxylic acid 3-methyl-but-2-enyl ester

(S)-Pyrrolidine-2-carboxylic acid 3-methyl-but-2-enyl ester

L-proline
147-85-3

L-proline

Conditions
ConditionsYield
With diethylamine; Pd(0) (in situ from Pd(OAc)2 and m.sulfonated triphenylphosphine) In water; acetonitrile for 0.75h;100%
1-(tert-butoxycarbonyl)-L-proline
15761-39-4

1-(tert-butoxycarbonyl)-L-proline

L-proline
147-85-3

L-proline

Conditions
ConditionsYield
With water at 170℃; for 0.05h; Microwave irradiation;100%
With tin(IV) chloride In ethyl acetate for 0.583333h; Ambient temperature;98%
With tetradecyl(trihexyl)phosphonium bistriflamide; trifluoroacetic acid at 130℃; for 0.166667h; Ionic liquid;96%
N-Benzyloxycarbonyl-L-proline
1148-11-4

N-Benzyloxycarbonyl-L-proline

L-proline
147-85-3

L-proline

Conditions
ConditionsYield
With hydrogen; palladium on activated charcoal In ethyl acetate at 80℃; for 0.0833333h; Microwave irradiation;100%
With hydrogen; hydroxyapatite-bound Pd In methanol at 40℃; for 1h;99%
With hydrogen; palladium on activated charcoal In ethyl acetate at 80℃; under 2585.81 Torr; for 0.0833333h; microwave irradiation;99%
Poc-Pro-OH
439912-48-8

Poc-Pro-OH

L-proline
147-85-3

L-proline

Conditions
ConditionsYield
With resin bound tetrathiomolybdate In methanol at 28℃; for 1.5h; ultrasonic bath;100%
D-Prolin
344-25-2

D-Prolin

L-proline
147-85-3

L-proline

Conditions
ConditionsYield
With porcine kidney D-amino acid oxidase (EC 1.4.3.3.); sodium cyanoborohydride; flavin adenine dinucleotide In phosphate buffer at 37℃;99%
lithium salicylate
552-38-5

lithium salicylate

A

Lithium Salicylate Proline

Lithium Salicylate Proline

B

L-proline
147-85-3

L-proline

Conditions
ConditionsYield
A n/a
B 99%
L-1-(chlorocarbonyl)proline ethyl ester
86050-92-2

L-1-(chlorocarbonyl)proline ethyl ester

L-proline
147-85-3

L-proline

Conditions
ConditionsYield
With hydrogenchloride at 25 - 75℃;98%
N-BOC-proline tert-butyl ester
91237-84-2

N-BOC-proline tert-butyl ester

L-proline
147-85-3

L-proline

Conditions
ConditionsYield
With hydrogenchloride In water at 20℃; for 2h;98%
With trifluoroacetic acid82%
(S)-methyl 1-(chlorocarbonyl)pyrrolidine-2-carboxylate
85665-59-4

(S)-methyl 1-(chlorocarbonyl)pyrrolidine-2-carboxylate

L-proline
147-85-3

L-proline

Conditions
ConditionsYield
With hydrogenchloride at 25 - 75℃;97%
Fmoc-Pro-OH
71989-31-6

Fmoc-Pro-OH

A

9-methylene-fluorene
4425-82-5

9-methylene-fluorene

B

L-proline
147-85-3

L-proline

Conditions
ConditionsYield
With dimethyl sulfoxide at 120℃; for 0.333333h;A n/a
B 96%
(3RS,6S)-3-[di(methoxycarbonyl)methyl]-1,6-trimethylene-2,5-piperazinedione
1319113-54-6

(3RS,6S)-3-[di(methoxycarbonyl)methyl]-1,6-trimethylene-2,5-piperazinedione

A

D-aspartic acid hydrochloride
71855-54-4

D-aspartic acid hydrochloride

B

L-aspartic acid hydrochloride
17585-59-0

L-aspartic acid hydrochloride

C

L-proline
147-85-3

L-proline

Conditions
ConditionsYield
With hydrogenchloride; water at 100℃; for 24h;A n/a
B n/a
C 95%
(2S)-N-allyloxycarbonyl-L-proline
110637-44-0

(2S)-N-allyloxycarbonyl-L-proline

A

L-proline
147-85-3

L-proline

B

(S)-1-allylproline
610299-77-9

(S)-1-allylproline

Conditions
ConditionsYield
With aminomethyl resin-supported N-propylbarbituric acid; tetrakis(triphenylphosphine) palladium(0) In tetrahydrofuran at 20 - 40℃;A 93%
B n/a
L-prolinamide
7531-52-4

L-prolinamide

L-proline
147-85-3

L-proline

Conditions
ConditionsYield
Stage #1: L-prolinamide With hydrogenchloride for 10h; Heating;
Stage #2: With methyloxirane In ethanol at 20℃; for 5h;
92%
Fmoc-Pro-OH
71989-31-6

Fmoc-Pro-OH

L-proline
147-85-3

L-proline

Conditions
ConditionsYield
With sodium azide In N,N-dimethyl-formamide at 50℃; for 3h;92%
C5H9NO2*H3N*ClH

C5H9NO2*H3N*ClH

L-proline
147-85-3

L-proline

Conditions
ConditionsYield
With ruthenium nanoparticles dispersed in a polyvinylpyrrolidone matrix; amberlyst A-21 In methanol; dichloromethane92%
L-prolinamide hydrochloride
42429-27-6

L-prolinamide hydrochloride

L-proline
147-85-3

L-proline

Conditions
ConditionsYield
With Amberlyst 15; water at 100℃; for 72h;90%
cinnamyl-L-prolinate

cinnamyl-L-prolinate

L-proline
147-85-3

L-proline

Conditions
ConditionsYield
With diethylamine; Pd(0) (in situ from Pd(OAc)2 and m.sulfonated triphenylphosphine) In water; acetonitrile for 0.666667h;86%
(S)-1-allylproline
610299-77-9

(S)-1-allylproline

L-proline
147-85-3

L-proline

Conditions
ConditionsYield
With aminomethyl resin-supported N-propylbarbituric acid; tetrakis(triphenylphosphine) palladium(0) In tetrahydrofuran at 40℃;86%
phenol
108-95-2

phenol

L-proline
147-85-3

L-proline

Conditions
ConditionsYield
86%
(3R,6S,1'RS)-3-(methoxycarbonylcyanomethyl)-1,6-trimethylene-2,5-piperazinedione
1319113-56-8

(3R,6S,1'RS)-3-(methoxycarbonylcyanomethyl)-1,6-trimethylene-2,5-piperazinedione

A

D-aspartic acid hydrochloride
71855-54-4

D-aspartic acid hydrochloride

B

L-proline
147-85-3

L-proline

Conditions
ConditionsYield
With hydrogenchloride; water at 100℃; for 24h;A 84%
B 82%
(S)-tetrahydro-3'H-9λ4-boraspiro[bicyclo[3.3.1]nonane-9,1'-pyrrolo[1,2-c][1,3,2]oxazaborol]-3'-one

(S)-tetrahydro-3'H-9λ4-boraspiro[bicyclo[3.3.1]nonane-9,1'-pyrrolo[1,2-c][1,3,2]oxazaborol]-3'-one

L-proline
147-85-3

L-proline

Conditions
ConditionsYield
With tetrabutyl ammonium fluoride In tetrahydrofuran; water at 20℃; for 7h;82%
(3R,8aS)-hexahydro-3-(prop-2-enyl)pyrrolo[1,2-a]pyrazine-1,4-dione
205875-07-6

(3R,8aS)-hexahydro-3-(prop-2-enyl)pyrrolo[1,2-a]pyrazine-1,4-dione

A

D-allylglycine
54594-06-8

D-allylglycine

B

L-proline
147-85-3

L-proline

Conditions
ConditionsYield
With hydrogenchloride at 90℃; for 10h;A 80%
B 62%
L-proline (+)-10-camphorsulfonic acid salt

L-proline (+)-10-camphorsulfonic acid salt

L-proline
147-85-3

L-proline

Conditions
ConditionsYield
With triethylamine In dichloromethane at 25℃; for 0.5h;78%
L-proline methanesulfonic acid salt

L-proline methanesulfonic acid salt

L-proline
147-85-3

L-proline

Conditions
ConditionsYield
With triethylamine In dichloromethane at 25℃; for 0.5h; Solvent;70%
L-ornithine
70-26-8

L-ornithine

L-proline
147-85-3

L-proline

Conditions
ConditionsYield
platinum(IV) oxide; Pt/titania In water for 41h; Irradiation; pH 9.8;43%
platinum(IV) oxide; Pt/titania In water for 41h; Product distribution; Irradiation; pH 9.8; other amino acids and derivatives; other catalyst and rection time;
With Pseudomonas putida N-methyl-L-amino acid dehydrogenase; T. viride L-lysine oxidase; Tris buffer; flavin adenine dinucleotide; catalase In various solvent(s) at 30℃; for 2h; pH=8.0;
With benzenesulfonamide; ornithine cyclodeaminase; NAD In various solvent(s) at 30℃; pH=8.0;
With NAD; dehydrogenase from Candida boidinii; pyrroline-5-carboxylate reductase from Halomonas elongata; transaminase from Halomonas elongata; 2-oxo-propionic acid In aq. buffer at 37℃; pH=10; Reagent/catalyst; Enzymatic reaction;
(S)-proline (S)-1,1'-bi-2-naphthol 1:2 complex

(S)-proline (S)-1,1'-bi-2-naphthol 1:2 complex

(S)-[1,1']-binaphthalenyl-2,2'-diol
18531-99-2

(S)-[1,1']-binaphthalenyl-2,2'-diol

B

L-proline
147-85-3

L-proline

Conditions
ConditionsYield
In water; ethyl acetate at 20℃; for 2h;A 42%
B 0.257 g
methanol
67-56-1

methanol

L-proline
147-85-3

L-proline

methyl (2S)-pyrrolidine carboxylate
2577-48-2

methyl (2S)-pyrrolidine carboxylate

Conditions
ConditionsYield
With hydrogenchloride for 2h; Heating;100%
With thionyl chloride Heating;100%
With sulfuryl dichloride100%
benzoyl chloride
98-88-4

benzoyl chloride

L-proline
147-85-3

L-proline

N-(benzoyl)-L-proline
5874-58-8

N-(benzoyl)-L-proline

Conditions
ConditionsYield
With sodium hydroxide In tetrahydrofuran at 0 - 20℃;100%
With sodium hydroxide In water at 0℃; for 2h;89%
With potassium carbonate In tetrahydrofuran at 60℃;85%
benzyl chloroformate
501-53-1

benzyl chloroformate

L-proline
147-85-3

L-proline

N-Benzyloxycarbonyl-L-proline
1148-11-4

N-Benzyloxycarbonyl-L-proline

Conditions
ConditionsYield
With sodium hydroxide In water for 13.5h; Ambient temperature;100%
With sodium carbonate at 0 - 20℃; for 3h;100%
With sodium hydroxide at 0℃; for 0.166667h;97%
p-toluenesulfonyl chloride
98-59-9

p-toluenesulfonyl chloride

L-proline
147-85-3

L-proline

L-N-tosyl-proline
51077-01-1, 110771-95-4

L-N-tosyl-proline

Conditions
ConditionsYield
With sodium carbonate Inert atmosphere;100%
With water; sodium hydroxide at 70℃; for 2h;99%
In sodium hydroxide98.3%
L-proline
147-85-3

L-proline

(S)-1-Pyrrolidin-2-yl-methanol
23356-96-9

(S)-1-Pyrrolidin-2-yl-methanol

Conditions
ConditionsYield
Stage #1: L-proline With lithium aluminium tetrahydride In tetrahydrofuran for 1.25h; Heating / reflux;
Stage #2: With potassium hydroxide In tetrahydrofuran; water for 1.25h; Heating / reflux;
100%
Stage #1: L-proline With lithium aluminium tetrahydride In tetrahydrofuran Inert atmosphere; Cooling with ice; Reflux;
Stage #2: With potassium hydroxide In tetrahydrofuran at 20℃; Reflux;
99%
With lithium aluminium tetrahydride In tetrahydrofuran at 0℃; for 72.5h; Reflux;99%
methanol
67-56-1

methanol

L-proline
147-85-3

L-proline

L-proline methyl ester monohydrochloride
2133-40-6

L-proline methyl ester monohydrochloride

Conditions
ConditionsYield
With thionyl chloride for 1.5h; Heating;100%
With hydrogenchloride for 4h; Ambient temperature;100%
With thionyl chloride for 1.5h; Heating;100%
isatoic anhydride
118-48-9

isatoic anhydride

L-proline
147-85-3

L-proline

(S)-1,2,3,11a-tetrahydro-5H-pyrrolo[2,1-c][1,4]benzodiazepine-5,11(10H)-dione
24919-40-2, 60269-66-1, 18877-34-4

(S)-1,2,3,11a-tetrahydro-5H-pyrrolo[2,1-c][1,4]benzodiazepine-5,11(10H)-dione

Conditions
ConditionsYield
In N,N-dimethyl-formamide at 160℃; for 4h;100%
In dimethyl sulfoxide at 180℃; Condensation;96%
In dimethyl sulfoxide at 100℃; for 4h;95%
ethanol
64-17-5

ethanol

L-proline
147-85-3

L-proline

L-proline ethyl ester monohydrochloride
33305-75-8

L-proline ethyl ester monohydrochloride

Conditions
ConditionsYield
With hydrogenchloride for 1h; Heating;100%
With thionyl chloride for 12h; Reflux; Green chemistry;99%
Stage #1: L-proline With thionyl chloride In ethanol for 6h; Heating;
Stage #2: ethanol Further stages.;
98%
di-tert-butyl dicarbonate
24424-99-5

di-tert-butyl dicarbonate

L-proline
147-85-3

L-proline

1-(tert-butoxycarbonyl)-L-proline
15761-39-4

1-(tert-butoxycarbonyl)-L-proline

Conditions
ConditionsYield
With sodium hydrogencarbonate In tetrahydrofuran; water at 20℃; for 19h; Cooling with ice;100%
With amberlyst-15 In ethanol at 20℃; for 0.0833333h; chemoselective reaction;100%
With sodium hydrogencarbonate In tetrahydrofuran; water at 0 - 20℃; for 16h;100%
methanol
67-56-1

methanol

chloroformic acid ethyl ester
541-41-3

chloroformic acid ethyl ester

L-proline
147-85-3

L-proline

(S)-proline-N-ethyl carbamate methyl ester
77581-28-3, 93423-88-2

(S)-proline-N-ethyl carbamate methyl ester

Conditions
ConditionsYield
With potassium carbonate In methanol100%
With potassium carbonate at 0 - 20℃;100%
With potassium carbonate at 0 - 20℃; for 7.5h; Inert atmosphere;100%
chloroformic acid ethyl ester
541-41-3

chloroformic acid ethyl ester

L-proline
147-85-3

L-proline

(S)-N-(ethoxycarbonyl)proline
5700-74-3

(S)-N-(ethoxycarbonyl)proline

Conditions
ConditionsYield
With sodium carbonate In tetrahydrofuran at 0℃; for 2h;100%
Stage #1: chloroformic acid ethyl ester; L-proline With sodium hydroxide; water at 0 - 20℃; pH=9 - 10;
Stage #2: With hydrogenchloride; water at 0℃; pH=1;
100%
With sodium hydrogencarbonate In water at 25℃; for 12h;96%
benzenesulfonyl chloride
98-09-9

benzenesulfonyl chloride

L-proline
147-85-3

L-proline

N-benzenesulfonyl-L-proline
88425-46-1

N-benzenesulfonyl-L-proline

Conditions
ConditionsYield
With sodium carbonate In water for 5h;100%
With sodium carbonate In water for 4h;100%
With sodium carbonate In water at -5 - 20℃; for 4h; Inert atmosphere;100%
ortho-toluoyl chloride
933-88-0

ortho-toluoyl chloride

L-proline
147-85-3

L-proline

N-(2-methylbenzoyl)-L-proline

N-(2-methylbenzoyl)-L-proline

Conditions
ConditionsYield
With sodium hydroxide for 0.5h;100%
With sodium hydroxide In tetrahydrofuran; water at 0 - 20℃;0.77 g
Conditions
ConditionsYield
With ferrous(II) sulfate heptahydrate; cis-3-proline hydroxylase type II; sodium L-ascorbate at 37℃; for 16h; stereospecific reaction;100%
With iron(II) sulfate; α-ketoglutaric acid disodium salt In culture medium at 28℃; for 72h; Enzymatic reaction; regioselective reaction;61%
With 4-morpholineethanesulfonic acid; α-ketoglutaric acid; bovine serum albumin; proline 3-hydroxylase; iron(II) sulfate In water pH=6.0; Oxidation; hydroxylation;
With hydrogenchloride; α-ketoglutaric acid; ammonium iron (II) sulfate; L-proline cis-3-hydroxylase type I; sodium L-ascorbate In aq. buffer at 21℃; for 14h; pH=6.5; Enzymatic reaction;> 95 %Chromat.
With ferrous(II) sulfate heptahydrate; α-ketoglutaric acid disodium salt; ascorbic acid In aq. phosphate buffer at 37℃; for 16h; pH=7.5; Enzymatic reaction;530 mg
tetra(n-butyl)ammonium hydroxide
2052-49-5

tetra(n-butyl)ammonium hydroxide

L-proline
147-85-3

L-proline

proline, tetrabutylammonium carboxylate salt

proline, tetrabutylammonium carboxylate salt

Conditions
ConditionsYield
In methanol at 0 - 20℃; for 3h; Inert atmosphere;100%
In methanol97%
In water at 20℃; for 2h;95%
ortho-nitrofluorobenzene
1493-27-2

ortho-nitrofluorobenzene

L-proline
147-85-3

L-proline

(S)-N-(2-nitrophenyl)proline
31981-54-1

(S)-N-(2-nitrophenyl)proline

Conditions
ConditionsYield
With sodium hydrogencarbonate In ethanol; water for 5h; Heating;100%
With sodium hydrogencarbonate In ethanol; water Heating;94%
With triethylamine In dimethyl sulfoxide80.3%
With sodium hydrogencarbonate In ethanol; water at 100℃;
Allyl chloroformate
2937-50-0

Allyl chloroformate

L-proline
147-85-3

L-proline

(2S)-N-allyloxycarbonyl-L-proline
110637-44-0

(2S)-N-allyloxycarbonyl-L-proline

Conditions
ConditionsYield
With sodium hydrogencarbonate In diethyl ether at 20℃; for 16h;100%
With hydrogenchloride; sodium hydroxide In tetrahydrofuran; water
N-benzyloxycarbonyl-(2S)-aminobutyric acid succinimide ester
71447-81-9

N-benzyloxycarbonyl-(2S)-aminobutyric acid succinimide ester

L-proline
147-85-3

L-proline

N-benzyloxycarbonyl-(2S)-aminobutyryl-L-proline
185212-64-0

N-benzyloxycarbonyl-(2S)-aminobutyryl-L-proline

Conditions
ConditionsYield
With triethylamine In tetrahydrofuran; water at 20℃;100%
3-benzo[b]thiophen-2-yl-3-tert-butoxycarbonylamino-propionic acid
776330-84-8

3-benzo[b]thiophen-2-yl-3-tert-butoxycarbonylamino-propionic acid

L-proline
147-85-3

L-proline

[1-benzo[b]thiophen-2-yl-3-(2-S-carbamoyl-pyrrolidin-1-yl)-3-oxo-propyl]-carbamic acid tert-butyl ester
776330-85-9

[1-benzo[b]thiophen-2-yl-3-(2-S-carbamoyl-pyrrolidin-1-yl)-3-oxo-propyl]-carbamic acid tert-butyl ester

Conditions
ConditionsYield
With benzotriazol-1-ol; N-(3-dimethylaminopropyl)-N-ethylcarbodiimide In DMF (N,N-dimethyl-formamide) at 20℃; for 2.5h;100%
C22H24N2O5
869882-73-5

C22H24N2O5

L-proline
147-85-3

L-proline

C27H33N3O7

C27H33N3O7

Conditions
ConditionsYield
In dichloromethane at 20℃; for 18h;100%
6-methyl-6-phenylfulvene
2320-32-3

6-methyl-6-phenylfulvene

L-proline
147-85-3

L-proline

A

salt of L-proline+6-methyyl-6-phenylfulvene

salt of L-proline+6-methyyl-6-phenylfulvene

B

α-phenethylcyclopentadiene

α-phenethylcyclopentadiene

Conditions
ConditionsYield
With n-butyllithiumA 100%
B n/a
L-proline
147-85-3

L-proline

L-proline methyl ester monohydrochloride
2133-40-6

L-proline methyl ester monohydrochloride

Conditions
ConditionsYield
With thionyl chloride In methanol at 20℃;100%
With sulfuryl dichloride; trimethyl orthoformate In methanol
With sulfuryl dichloride; trimethyl orthoformate In methanol
With sulfuryl dichloride; trimethyl orthoformate In methanol
di(μ-chloro)bis[1-(phenylazo)phenyl-C(2)N]dipalladium(II)
14873-53-1

di(μ-chloro)bis[1-(phenylazo)phenyl-C(2)N]dipalladium(II)

L-proline
147-85-3

L-proline

Pd(C6H4NNC6H5)(NHC4H7CO2)

Pd(C6H4NNC6H5)(NHC4H7CO2)

Conditions
ConditionsYield
With NaOMe In methanol N2-atmosphere; dropwise addn. of 1 equiv. NaOMe to aminoacid, gentle heating to dissoln., addn. of stoich. amt. Pd-complex, stirring for 15 h; solvent removal (vac.), dissoln. in CH2Cl2, centrifugation, solvent removal (vac.), repeated recrystn. (CH2Cl2/hexane); elem. anal.;100%
1,3-cylohexanedione
504-02-9

1,3-cylohexanedione

L-proline
147-85-3

L-proline

1-(3-oxocyclohex-1-enyl)pyrrolidine-2-carboxylic acid
1033193-52-0

1-(3-oxocyclohex-1-enyl)pyrrolidine-2-carboxylic acid

Conditions
ConditionsYield
In benzene for 5h; Reflux;100%
toluene-4-sulfonic acid
104-15-4

toluene-4-sulfonic acid

L-proline
147-85-3

L-proline

benzyl alcohol
100-51-6

benzyl alcohol

L‑proline benzyl ester p‑toluenesulfonate
32302-87-7

L‑proline benzyl ester p‑toluenesulfonate

Conditions
ConditionsYield
In tetrachloromethane for 24h; Reflux;100%
In cyclohexane for 4h; Solvent; Fischer-Speier Esterification; Reflux; Dean-Stark;100%

147-85-3Related news

Synthesis and allosteric modulation of the dopamine receptor by peptide analogs of l-prolyl-l-leucyl-glycinamide (PLG) modified in the L-Proline (cas 147-85-3) or L-Proline (cas 147-85-3) and l-leucine scaffolds09/29/2019

Novel analogs of l-prolyl-l-leucylglycinamide (PLG) were synthesized wherein the prolyl residue was replaced with other amino acids based on a 3,5-disubstituted proline scaffold. In some examples, the l-leucyl residue was also replaced by l-valine. These analogs were tested for their ability to ...detailed

147-85-3Relevant articles and documents

Optical resolution, characterization, and X-ray crystal structures of diastereomeric salts of chiral amino acids with (S)-(-)-1-phenylethanesulfonic acid

Yoshioka,Ohtsuki,Da-Te,Okamura,Senuma

, p. 3012 - 3020 (1994)

Ten DL-Amino acids (AA), including neutral, and basic amino acids, and an imino acid, were optically resolved, without derivatization into their covalent compounds, by means of fractional crystallization of their diastereomeric salts with (-)-1-phenylethanesulfonic acid (PES) in various solvents. Several pairs of the diastereomeric crystalline salts formed during the resolutions were analyzed by DSC and spectroscopy, which showed that the successful resolutions were attributable to differences in various physicochemical properties between the more-soluble D-AA · (-)-PES and less-soluble L-AA · (-)-PES. Chiral recognition of the most successfully resolved species, DL-p-hydroxyphenylglycine (HPG) salt, was explored by comparing the X-ray crystal structures of D- and L-HPG · (-)-PES. The two crystal structures differed obviously in their hydrogen-bonding networks: the less-soluble L-HPG · (-)-PES only had strong hydrogen-bonded infinite chains of HPG in a 'head-to-tail' arrangement through the p-hydroxyl group, the structure of which was more geometrically stable than that of the more-soluble D-HPG · (-)-PES. The differences in the two crystal structures related to striking differences in their solubilities and thermal properties.

The relative catalytic efficiency of β-lactamase catalyzed acyl and phosphyl transfer

Slater, Martin J.,Laws, Andrew P.,Page, Michael I.

, p. 77 - 95 (2001)

Phosphonamidates which bear a simple resemblance to penicillin type structures have been synthesised as potential inhibitors of β-lactamases: -ethyl N-(benzyloxycarbonyl) amidomethyl phosphonyl amides, PhCH2OCONHCH2P(O)(OEt)NR2, the amines HNR2 being L-proline, D-proline, L-thiazolidine, and o-anthranilic acid. The proline derivatives completely and irreversibly inactivated the class C β-lactamase from Enterobacter cloacae P99, in a time-dependent manner, indicative of covalent inhibition. The inactivation was found to be exclusive to the class C enzyme and no significant inhibition was observed with any other class of β-lactamase. The anthranilic acid derivative exhibited no appreciable inactivation of the β-lactamases. The phosphonyl proline and phosphonyl thioproline derivatives were separated into their diastereoisomers and their individual second order rate constants for inhibition were found to be 7.72 ± 0.37 and 8.3 × 10-2 ± 0.004 M-1 s-1 for the L-proline derivatives, at pH 7.0. The products of the inhibition reaction of each individual diastereoisomer, analyzed by electrospray mass spectroscopy, indicate that the more reactive diastereoisomers phosphonylate the enzyme by P-N bond fission with the elimination of proline. Conversely, gas chromatographic detection of ethanol release by the less reactive proline diastereoisomer suggests phosphonylation occurs by P-O bond fission. The enzyme enhances the rate of phosphonylation with P-N fission by at least 106 compared with that effected by hydroxide-ion. The pH dependence of the rate of inhibition of the β-lactamase by the more reactive diasteroisomer is consistent with the reaction of the diprotonated form of the enzyme, EH2, with the inhibitor, I (or its kinetic equivalents EH with IH). This pH dependence and the rate enhancement indicate that the enzyme appears to use the same catalytic apparatus for phosphonylation as that used for hydrolysis of β-lactams. The stereochemical consequences of nucleophilic displacement at the phosphonyl centre are discussed.

Viridamides A and B, lipodepsipeptides with antiprotozoal activity from the marine cyanobacterium Oscillatoria nigro-viridis

Simmons, T. Luke,Engene, Niclas,Urena, Luis David,Romero, Luz I.,Ortega-Barria, Eduardo,Gerwick, Lena,Gerwick, William H.

, p. 1544 - 1550 (2008)

Parallel chemical and phylogenetic investigation of a marine cyanobacterium from Panama led to the isolation of two new PKS-NRPS-derived compounds, viridamides A and B. Their structures were determined by NMR and mass spectroscopic methods, and the absolute configurations assigned by Marfey's method and chiral HPLC analysis. In addition to six standard, N-methylated amino and hydroxy acids, these metabolites contained the structurally novel 5-methoxydec-9-ynoic acid moiety and an unusual proline methyl ester terminus. Morphologically, this cyanobacterium was identified as Oscillatoria nigro-viridis, and its 16S rDNA sequence is reported here for the first time. Phylogenetic analysis of these sequence data has identified O. nigro-viridis strain OSC3L to be closely related to two other marine cyanobacterial genera, Trichodesmium and Blennothrix. Viridamide A showed antitrypanosomal activity with an IC50 of 1.1 μM and antileishmanial activity with an IC50 of 1.5 μM.

Structures and solution conformational dynamics of stylissamides G and H from the Bahamian Sponge Stylissa caribica

Wang, Xiao,Morinaka, Brandon I.,Molinski, Tadeusz F.

, p. 625 - 630 (2014)

Two new peptides, stylissamides G and H, were isolated from extracts of a sample of Stylissa caribica collected in deep waters of the Caribbean Sea. A single sample of S. caribica among a collection of 10 samples that were examined by LC-MS appeared to be a different chemotype from the others in that it lacked the familiar pyrrole-2-aminoimidazole alkaloids, stevensine and oroidin, and contained peptides of the stylissamide class. The structures of the title compounds were solved by integrated analysis of the MS and NMR spectra and chemical degradation. The solution conformation of stylissamide G was briefly examined by electronic circular dichroism and temperature-dependent 1H NMR chemical shifts of amide NH signals, which supported a conformationally rigid macrocycle.

Heterogeneous Asymmetric Hydrogenation of a Chiral Tripeptide containing Dehydroalanine and α,β-Dehydrobutyrine Residues

Takasaki, Michiaki,Harada, Kaoru

, p. 571 - 573 (1987)

The heterogeneous asymmetric hydrogenation of a linear tripeptide containing dehydroalanine and α,β-dehydrobutyrine has been carried out, giving asymmetric yields of alanine and butyrine of 94 and 54percent, respectively.

New diketopiperazine derivatives isolated from sea urchin-derived Bacillus sp.

Yonezawa, Ken,Yamada, Koji,Kouno, Isao

, p. 106 - 108 (2011)

Two new diketopiperazine derivatives, bacillusamides A (1) and B (2), have been isolated from the EtOAc extract of the sea urchin-derived Bacillus sp. along with the known cyclo(-L-pro-L-val-) (3), cyclo(-L-pro-L-tyr-) (4), cyclo(-L-pro-L-phe-) (5). These structures were elucidated by extensive spectroscopic methods. Furthermore, the absolute configurations of the amino acid residues were determined using Marfey's method. Compound 1 displayed weak antifungal activity against Aspergillus niger.

Cipralphelin, a new anti-oxidative N-cinnamoyl tripeptide produced by the deep sea-derived fungal strain Penicillium brevicompactum FKJ-0123

Matsuo, Hirotaka,Mokudai, Takayuki,Higo, Mayuka,Nonaka, Kenichi,Nagano, Yuriko,Nagahama, Takahiko,Niwano, Yoshimi,Takahashi, Yōko,ōmura, Satoshi,Nakashima, Takuji

, p. 775 - 778 (2019)

A new N-cinnamoyl tripeptide, designated cipralphelin (1), was isolated from a cultured broth of Penicillium brevicompactum FKJ-0123 by physicochemical (PC) screening. Compound 1 was purified by silica gel and ODS column chromatography followed by preparative HPLC. The structure of 1 was determined as N-cinnamoyl-prolyl-alanyl-phenylalanine methyl ester by nuclear magnetic resonance and mass spectrometry analyses. The absolute configurations of three amino acids were determined by an advanced Marfey’s method applied to the hydrolysate of 1. Compound 1 was evaluated for its cytotoxicity, anti-microbial activity, and ability to scavenge or quench reactive oxygen species (ROS) such as superoxide anion radicals, hydroxy radicals, and singlet oxygen. Compound 1 exhibited potent scavenging activity against hydroxy radicals.

Dudawalamides A-D, Antiparasitic Cyclic Depsipeptides from the Marine Cyanobacterium Moorea producens

Almaliti, Jehad,Malloy, Karla L.,Glukhov, Evgenia,Spadafora, Carmenza,Gutiérrez, Marcelino,Gerwick, William H.

, p. 1827 - 1836 (2017)

A family of 2,2-dimethyl-3-hydroxy-7-octynoic acid (Dhoya)-containing cyclic depsipeptides, named dudawalamides A-D (1-4), was isolated from a Papua New Guinean field collection of the cyanobacterium Moorea producens using bioassay-guided and spectroscopic approaches. The planar structures of dudawalamides A-D were determined by a combination of 1D and 2D NMR experiments and MS analysis, whereas the absolute configurations were determined by X-ray crystallography, modified Marfey's analysis, chiral-phase GCMS, and chiral-phase HPLC. Dudawalamides A-D possess a broad spectrum of antiparasitic activity with minimal mammalian cell cytotoxicity. Comparative analysis of the Dhoya-containing class of lipopeptides reveals intriguing structure-activity relationship features of these NRPS-PKS-derived metabolites and their derivatives.

Synergie effect of two metal centers in catalytic hydrolysis of methionine-containing peptides promoted by dinuclear palladium(II) hexaazacyclooctadecane complex

Yang, Gaosheng,Miao, Ren,Li, Yizhi,Hong, Jing,Zhao, Chuenmei,Guo, Zijian,Zhu, Longgen

, p. 1613 - 1619 (2005)

The species obtained by the reaction of [Pd2([18]aneN 6)Cl2](ClO4)2 (where [18]aneN 6 is 1,4,7,10,13,16-hexaazacyclooctadecane) with AgBF4 have been determined by electrospray ionization mass spectrometry (ESI-MS) to be an equilibrium mixture of three major types of dinuclear Pd(II) complex cations, [Pd2(-O)([18]aneN6)]2+, [Pd 2(μ-OH)-([18]aneN6)]3+ and [Pd 2(H2O)(OH)([18]aneN6)]3+, in aqueous solution. The hydroxo-group-bridged one, [Pd2(μ-OH)-([18] aneN6)]3+, is a dominant species, whose crystal structure has been obtained. The crystal structure of [Pd2(μ-OH)-([18] aneN6)](ClO4)3 shows that each Pd(II) ion in the dinuclear complex is tetra-coordinated by three nitrogen atoms and one hydroxo group bridge in a distorted square configuration. The two Pd(II) ions are 3.09 A apart from each other. The dinuclear Pd(II) complex cations [Pd2(μ-OH)([18]aneN6)]3+ and [Pd 2(H2O)(OH)([18]aneN6)]3+ can efficiently catalyze hydrolysis of the amide bond involving the carbonyl group of methionine in methionine-containing peptides with turnover number of larger than 20. In these hydrolytic reactions, the two Pd(II) ions are synergic; one Pd(II) ion anchors to the side chain of methionine and the other one delivers hydroxo group or aqua ligand to carbonyl carbon of methionine, or acts as a Lewis acid to activate the carbonyl group of methionine, resulting in cleavage of Met-X bond. The binding constant of dinuclear Pd(II) complex cations with AcMet-Gly and AcMet were determined by 1H NMR titration to be 282±2 M-1 and 366±4 M-1, respectively. The relatively low binding constants enable the catalytic cycle and the possible catalytic mechanism is proposed. This is the first artificial mimic of metallopeptidases with two metal active centers. The Royal Society of Chemistry 2005.

Isolation and synthesis of falcitidin, a novel myxobacterial-derived acyltetrapeptide with activity against the malaria target falcipain-2

Somanadhan, Brinda,Kotturi, Santosh R.,Yan Leong, Chung,Glover, Robert P.,Huang, Yicun,Flotow, Horst,Buss, Antony D.,Lear, Martin J.,Butler, Mark S.

, p. 259 - 264 (2013)

A 384-well microtitre plate fluorescence cleavage assay was developed to identify inhibitors of the cysteine protease falcipain-2, an important antimalarial drug target. Bioassay-guided isolation of a MeOH extract from a myxobacterium Chitinophaga sp. Y23 isolated from soil collected in Singapore, led to the identification of a new acyltetrapeptide, falcitidin (1), which displayed an IC 50 value of 6 μM against falcipain-2. The planar structure of 1 was secured by NMR and MS/MS analysis. Attempts to isolate further material for biological testing were hampered by inconsistent production and by a low yield (100 μg l -1). The absolute configuration of 1 was determined by Marfey's analysis and the structure was confirmed through total synthesis as isovaleric acid-D-His-L-Ile-L-Val-L-Pro-NH 2. Falcitidin (1) is the first member of a new class of falcipain-2 inhibitors and, unlike other peptide-based inhibitors, does not contain reactive groups that irreversibly bind to active cysteine sites.

Tunicyclin a, the first plant tricyclic ring cycloheptapeptide from Psammosilene tunicoides

Tian, Jun-Mian,Shen, Yun-Heng,Yang, Xian-Wen,Liang, Shuang,Tang, Jian,Shan, Lei,Zhang, Wei-Dong

, p. 1131 - 1133 (2009)

A novel cycloheptapeptide, tunicyclin A, with a unique tricyclic ring cyclopeptide skeleton, was isolated from Psammosilene tunicoides. Its structure was elucidated by extensive NMR and MS analysis. Biogenetically, tunicyclin A might be derived from cyclo

Specialized metabolites from the aerial parts of Centaurea polyclada DC.

Demir, Serdar,Karaalp, Canan,Bedir, Erdal

, p. 12 - 18 (2017)

The genus Centaurea L. (Asteraceae) is represented by 200 taxa in the flora of Turkey and several Centaurea species are used as herbal remedies against different conditions. Previous phytochemical investigations on this genus generally revealed the isolation of sesquiterpene lactones and flavonoid derivatives. In our continuous search on Centaurea genus, a phytochemical study was performed on Centaurea polyclada DC., an endemic of West Anatolia. Previously undescribed two sesquiterpene-amino acid conjugates, an elemane and an eudesmane derivative were isolated from the aerial parts of Centaurea polyclada, together with eight known compounds; two elemane derivatives, three flavonoids, a lignan, a phenolic glucoside and a phenylpropanoid glucoside. Structural elucidation of the compounds was based on spectroscopic evidence, including 1D and 2D NMR and high-resolution mass spectrometry, chemical degradation results and reference data comparison. Sesquiterpene-amino acid conjugates are representatives of an unusual group of sesquiterpenes, and elemane-amino acid conjugates are herein reported for the first time in nature.

Jahanyne, an apoptosis-inducing lipopeptide from the marine cyanobacterium lyngbya sp.

Iwasaki, Arihiro,Ohno, Osamu,Sumimoto, Shinpei,Ogawa, Hidetoshi,Nguyen, Kim Anh,Suenaga, Kiyotake

, p. 652 - 655 (2015)

An acetylene-containing lipopeptide, jahanyne, was isolated from the marine cyanobacterium Lyngbya sp. Its gross structure was established by spectroscopic analyses, and the absolute configuration was clarified based on a combination of chiral HPLC analyses, spectroscopic analyses, and derivatization reactions. Jahanyne significantly inhibited the growth of human cancer cells and induced apoptosis in HeLa cells.

STRUCTURE OF CYCLOTHIAZOMYCIN, A UNIQUE POLYTHIAZOLE-CONTAINING PEPTIDE WITH RENIN INHIBITORY ACTIVITY. PART 1. CHEMISTRY AND PARTIAL STRUCTURES OF CYCLOTHIAZOMYCIN

Aoki, Masahiro,Ohtsuka, Tatsuo,Itezono, Yoshiko,Yokose, Kazuteru,Furihata, Kazuo,Seto, Haruo

, p. 217 - 220 (1991)

Cyclothiazomycin is a novel renin inhibitor produced by Streptomyces sp.NR 0516 (IC50 1.66μM).Its molecular formular was determined to be C59H64N18O14S7 (MW. 1472) based on high-resolution FAB mass and NMR spectroscopy.Five fragments of cyclothiazomycin containing thiazole, thiazoline, heterocyclic chromophore were clarified by extensive 2D-NMR experiments.

Stylissamides e and F, cyclic heptapeptides from the caribbean sponge stylissa caribica

Cychon, Christine,Koeck, Matthias

, p. 738 - 742 (2010)

In addition to the four known stylissamides, A (1), B (2), C, and D, two new cyclic heptapeptides, stylissamides E (3) and F (4), were isolated from the Caribbean sponge Stylissa caribica. The structures of 3 and 4 were elucidated from a combination of mass spectrometric and NMR spectroscopic data as cyclo-(cis-Pro1-Tyr2-trans-Pro3-Ala 4-Ile5-Gln6-Ile7) for stylissamide E (3) and cyclo-(trans-Pro1-cis-Pro2-Phe 3-Asp4-trans-Pro5-Arg6-Phe 7) for stylissamide F (4).

Ionic Liquids Derived from Proline: Application as Surfactants

Fernández-Stefanuto, Verónica,Corchero, Raquel,Rodríguez-Escontrela, Iria,Soto, Ana,Tojo, Emilia

, p. 2885 - 2893 (2018)

Ionic liquids derived from prolinium esters, previously described as fully green and stable, were found to decompose in the presence of water by ester hydrolysis. To avoid this problem, a new family of these biodegradable salts incorporating an alcohol instead of the ester group is proposed. From this family, two novel ionic liquids that incorporate the prolinolium cation [HOPro] and the [DS] or [DBS] anion were selected (DS=dodecylsulfate; DBS=dodecylbenzenesulfonate). Both salts are liquid at room temperature, a property not usually found in ionic surfactants, and are also chemically and thermally stable. Moreover, they are more effective in reducing the surface tension of water than the corresponding traditional surfactants in the form of sodium salts, being useful for applications related to their aggregation capacity. They were tested for surfactant enhanced oil recovery and an optimal formulation for reservoirs at high salinity and temperature, able to produce ultra-low interfacial tension, was found with [HOPro][DBS].

(-)/(+)-Sparteine induced chirally-active carbon nanoparticles for enantioselective separation of racemic mixtures

Vulugundam, Gururaja,Misra, Santosh K.,Ostadhossein, Fatemeh,Schwartz-Duval, Aaron S.,Daza, Enrique A.,Pan, Dipanjan

, p. 7513 - 7516 (2016)

Chiral carbon nanoparticles (CCNPs) were developed by surface passivation using the chiral ligand (-)-sparteine or (+)-sparteine (denoted (-)-SP/CNP and (+)-SP/CNP, respectively). The chirality of the prepared CCNPs was demonstrated by circular dichroism

An angiogenesis inhibitor isolated from a marine-derived actinomycete, Nocardiopsis sp. 03N67

Shin, Hee Jae,Mondol, M.A. Mojid,Yu, Tae Kyung,Lee, Hyi-Seung,Lee, Yeon-Ju,Jung, Hye Jin,Kim, Jong Hyeon,Kwon, Ho Jeong

, p. 194 - 197 (2010)

Cyclo-(l-Pro-l-Met) was isolated from the fermentation broth of a marine-derived actinomycete Nocardiopsis sp. 03N67 by chromatographic analysis and showed anti-angiogenesis activity against human umbilical vein endothelial cells (HUVECs). The structure and absolute stereochemistry of this compound were determined based on extensive spectroscopic data analysis, and Marfey's method, respectively.

Planktocyclin, a cyclooctapeptide protease inhibitor produced by the freshwater cyanobacterium Planktothrix rubescens

Baumann, Heike I.,Keller, Simone,Wolter, Falko E.,Nicholson, Graeme J.,Jung, Guenther,Suessmuth, Roderich D.,Juettner, Friedrich

, p. 1611 - 1615 (2007)

The freshwater cyanobacterium Planktothrix rubescens produces the cyclooctapeptide cyclo(Pro-Gly-Leu-Val-Met-Phe-Gly-Val). The chemical structure is new. This homodetic cyclic octapeptide was named planktocyclin (1). It consists solely of proteinogenic L-amino acids and is a strong inhibitor of mammalian trypsin and α-chymotrypsin and a moderately active inhibitor of human recombinant caspase-8. Mass spectrometric and 2D-NMR spectroscopic data allowed the determination of its structure. Synthetic planktocyclin was identical to the natural product.

Aestuaramides, a natural library of cyanobactin cyclic peptides resulting from isoprene-derived Claisen rearrangements

McIntosh, John A.,Lin, Zhenjian,Tianero, Ma. Diarey B.,Schmidt, Eric W.

, p. 877 - 883 (2013)

We report 12 cyanobactin cyclic peptides, the aestuaramides, from the cultivated cyanobacterium Lyngbya aestuarii. We show that aestuaramides are synthesized enzymatically as reverse O-prenylated tyrosine ethers that subsequently undergo a Claisen rearrangement to produce forward C-prenylated tyrosine. These results reveal that a nonenzymatic Claisen rearrangement dictates isoprene regiochemistry in a natural system. They also reveal one of the mechanisms that organisms use to generate structurally diverse compound libraries starting from simple ribosomal peptide pathways (RiPPs).

Chromatographic method for the determination of conditional equilibrium constants for the carbamate formation reaction from amino acids and peptides in aqueous solution

Chen, Jian-Ge,Sandberg, Mats,Weber, Stephen G.

, p. 7343 - 7350 (1993)

A novel and sensitive method has been developed and evaluated for the study of carbamate formation equilibria of amino acids and peptides in aqueous solution. The method is based on reversed-phase liquid chromatography with cetyltrimethylammonium bromide. The reliability of the method was established by comparing the results determined from the present study with the few data in the literature. The relaxation rate of the carbamate reaction was shown to be faster than the chromatographic distribution relaxation rate (seconds). As a result, the retention time of amine solutes is increased in the presence of CO2. Carbamate formation constants and mole fractions of carbamates at physiological pH of eleven L-α-amino acids and peptides were determined. No correlation between the formation constant and the ammonium pKa was found. There is significant dependence of the amount of a particular amino acid or peptide that exists as carbamate at pH 7.4 on the pKa of the ammonium group, however. This is due to mass action rather than reflecting the influence of pKa on the propensity of the amine to react with CO2. It is suggested that amino acids and peptides with ammonium pKa greater than 9.5 do not form significant amounts of carbamates in aqueous solution near neutral pH.

Urumamide, a novel chymotrypsin inhibitor with a β-amino acid from a marine cyanobacterium Okeania sp.

Kanamori, Yuki,Iwasaki, Arihiro,Sumimoto, Shinpei,Suenaga, Kiyotake

, p. 4213 - 4216 (2016)

Urumamide, a novel cyclic depsipeptide that contains a β-amino acid, was isolated from a marine cyanobacterium Okeania sp. Its gross structure was determined by spectroscopic analyses, and the absolute configuration was established based on Marfey's analyses and chiral HPLC analyses of hydrolysis products. Biologically, urumamide inhibited the growth of human cancer cells. In addition, urumamide inhibited chymotrypsin.

Odobromoamide, a terminal alkynyl bromide-containing cyclodepsipeptide from the marine cyanobacterium okeania sp.

Sueyoshi, Kosuke,Kudo, Takafumi,Yamano, Aki,Sumimoto, Shimpei,Iwasaki, Arihiro,Suenaga, Kiyotake,Teruya, Toshiaki

, p. 436 - 440 (2017)

The bioassay-guided fractionation of the Okinawan marine cyanobacterium Okeania sp. led to the isolation of the novel cyclodepsipeptide odobromoamide (1). The gross structure of 1 was determined by spectroscopic analyses, and its absolute stereochemistry was determined using a variety of different methods, including chemical derivatization and degradation followed by HPLC analysis. In addition, odobromoamide (1) exhibited broad-spectrum cytotoxicity against a human cancer cell line panel.

Porpoisamides A and B, two novel epimeric cyclic depsipeptides from a Florida Keys collection of Lyngbya sp.

Meickle, Theresa,Gunasekera, Sarath P.,Liu, Yanxia,Luesch, Hendrik,Paul, Valerie J.

, p. 6576 - 6580 (2011)

NMR-guided fractionation of a non-polar extract of a Florida Keys collection of Lyngbya sp. resulted in the isolation of two novel epimeric cyclic depsipeptides, porpoisamides A (1) and B (2). The planar structures of these compounds were determined using NMR spectroscopic techniques. The absolute configurations of amino and hydroxy acid subunits were assigned by enantioselective HPLC analysis. These compounds showed weak cytotoxicity towards HCT-116 colorectal carcinoma and U2OS osteosarcoma cells. The porpoisamides are a unique pair of cyclic depsipeptides that are epimeric at C-2 of the β-amino acid, 3-amino-2-methyloctanoic acid.

Selective activation of organocatalysts by specific signals

Maity, Chandan,Trausel, Fanny,Eelkema, Rienk

, p. 5999 - 6005 (2018)

Reminiscent of signal transduction in biological systems, artificial catalysts whose activity can be controlled by physical or chemical signals would be of high interest in the design of chemical systems that can respond to their environment. Self-immolative chemistry offers a generic method for the development of catalysts that can be activated by different signals. To demonstrate the versatility of that concept, we synthesized organocatalysts that can be activated by three different signals and that can be used to control two different reactions. In this way the organocatalyst proline is designed as a pro-catalyst that is activated either by the chemical signal H2O2, by light or by the enzyme penicillin acylase. The pro-catalysts were used to exert temporal control over the rate of an aldol reaction and a Michael reaction.

Squamins C–F, four cyclopeptides from the seeds of Annona globiflora

Sosa-Rueda, Javier,Domínguez-Meléndez, Vanihamin,Ortiz-Celiseo, Araceli,López-Fentanes, Fernando C.,Cuadrado, Cristina,Fernández, José J.,Daranas, Antonio Hernández,Cen-Pacheco, Francisco

, (2021/08/04)

Four cyclic octapeptides, squamins C–F, were isolated from the seeds of Annona globiflora Schltdl. These compounds share part of their amino acid sequence, -Pro-Met(O)-Tyr-Gly-Thr-, with previously reported squamins A and B. Their structures were determined using NMR spectroscopic techniques together with quantum mechanical calculations (QM-NMR), ESI-HRMS data and a modified version of Marfey's chromatographic method. All compounds showed cytotoxic activity against DU-145 (human prostate cancer) and HeLa (human cervical carcinoma) cell lines. Clearly, A. globiflora is an important source of bioactive molecules, which could promote the sustainable exploitation of this undervalued specie.

Direct monitoring of biocatalytic deacetylation of amino acid substrates by1H NMR reveals fine details of substrate specificity

De Cesare, Silvia,McKenna, Catherine A.,Mulholland, Nicholas,Murray, Lorna,Bella, Juraj,Campopiano, Dominic J.

supporting information, p. 4904 - 4909 (2021/06/16)

Amino acids are key synthetic building blocks that can be prepared in an enantiopure form by biocatalytic methods. We show that thel-selective ornithine deacetylase ArgE catalyses hydrolysis of a wide-range ofN-acyl-amino acid substrates. This activity was revealed by1H NMR spectroscopy that monitored the appearance of the well resolved signal of the acetate product. Furthermore, the assay was used to probe the subtle structural selectivity of the biocatalyst using a substrate that could adopt different rotameric conformations.

Genomics-driven discovery of a new cyclodepsipeptide from the guanophilic fungusAmphichorda guana

Liang, Min,Lyu, Hai-Ning,Ma, Zi-Ying,Li, Er-Wei,Cai, Lei,Yin, Wen-Bing

, p. 1960 - 1964 (2021/03/16)

Two potential non-ribosomal peptide synthetases (NRPSs) were identified in the genome of a guanophilic fungusAmphichorda guanaby bioinformatics analysis and gene knockout experiments. Liquid chromatography coupled with mass spectrometry (LC-MS) guided isolation led to the discovery of a new cyclodepsipeptide isaridin H (1) and seven known analogs, desmethylisaridin E (2), isaridin E (3), isariin A (4), iso-isariin B (5), iso-isariin D (6), isariin E (7), and nodupetide (8). The absolute configuration of isaridin H (1) was achieved by Marfey's method. Isaridin H (1) showed significant antifungal activity againstBotrytis cinereaandAlternaria solani.

Post a RFQ

Enter 15 to 2000 letters.Word count: 0 letters

Attach files(File Format: Jpeg, Jpg, Gif, Png, PDF, PPT, Zip, Rar,Word or Excel Maximum File Size: 3MB)

1

What can I do for you?
Get Best Price

Get Best Price for 147-85-3