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L-Proline is a non-essential amino acid that serves as a crucial building block for proteins. It is unique among the twenty DNA-encoded amino acids, as it has a secondary amino group alpha to the carboxyl group. L-Proline plays a significant role in the formation of collagen, which is vital for the proper functioning of joints, tendons, and heart muscles. It is also recognized for its osmoprotectant properties and is used in various applications across different industries.

147-85-3

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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.

Uses

Used in Pharmaceutical and Biotechnological Applications:
L-Proline is used as an asymmetric catalyst in organic synthesis and asymmetric aldol cyclization. It is involved in the Michael addition of dimethyl malonate to alfa-beta-unsaturated aldehydes. Due to its osmoprotectant property, it finds uses in pharmaceutical and biotechnological applications, including the commercial biomanufacturing of therapeutic recombinant proteins and monoclonal antibodies.
Used in Collagen Production:
L-Proline, along with vitamin C, serves as a precursor for collagen, which is the primary component of the structure of tendons, ligaments, arteries, veins, and muscles. It is essential for wound healing and maintaining the integrity of connective tissues.
Used in Cell Culture Media:
L-Proline is utilized as a component of cell culture media for the commercial production of therapeutic recombinant proteins and monoclonal antibodies, making it a valuable asset in the biomanufacturing industry.
Used in Chromatography:
L-Proline is used in conjunction with ninhydrin in chromatography, a technique used to separate and analyze the components of a mixture.
Used in Nutritional Applications:
L-Proline is an ingredient in infusion and infant formula, providing essential nutrition to infants and patients requiring intravenous feeding.
Used in Quality Control:
Pharmaceutical secondary standards containing L-Proline are used for quality control in pharmaceutical laboratories and manufacturing, offering a convenient and cost-effective alternative to the preparation of in-house working standards.
Physical Properties:
L-Proline is an odorless or slightly odorous, slightly sweet-tasting amino acid. It is synthesized from L-glutamine and L-glutamate via L-ornithine in the intestine and liver. It is widely found as a component in many proteins and occurs as the free acid in natural products, making it a major constituent of collagen, the main fibrous protein found in bone, cartilage, and other connective tissues.
Chemical Properties:
L-Proline is a colorless to white crystal or crystalline powder at room temperature. It is soluble in water but insoluble in ethanol, diethyl ether, and n-butanol. It exhibits a yellow color in the presence of hydrated ninhydrin test solution and turns red after acidification with glacial acetic acid. The pH of L-Proline is 6.3, and its decomposition point is 220-222°C. The specific optical rotation of L-Proline is [α]20D-85° (0.5-2.0mg/ml, H2O) and [α]20D-60.4° (0.5-2.0mg /ml, 5mol/L HCl).

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.

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.

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

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  • (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.

Tasiamide F, a potent inhibitor of cathepsins D and E from a marine cyanobacterium

Al-Awadhi, Fatma H.,Ratnayake, Ranjala,Paul, Valerie J.,Luesch, Hendrik

, p. 3276 - 3282 (2016)

In search of novel protease inhibitors with therapeutic potential, our efforts exploring the marine cyanobacterium Lyngbya sp. have led to the discovery of tasiamide F (1), which is an analogue of tasiamide B (2). The structure was elucidated using a combination of NMR spectroscopy and mass spectrometry. The key structural feature in 1 is the presence of the Phe-derived statine core, which contributes to its aspartic protease inhibitory activity. The antiproteolytic activity of 1 and 2 was evaluated in vitro against cathepsins D and E, and BACE1. Tasiamide F (1) displayed IC50values of 57?nM, 23?nM, and 0.69?μM, respectively, indicating greater selectivity for cathepsins over BACE1 compared with tasiamide B (2). Molecular docking experiments were carried out for compounds 1 and 2 against cathepsins D and E to rationalize their activity towards these proteases. The dysregulated activities of cathepsins D and E have been implicated in cancer and modulation of immune responses, respectively, and these proteases represent potential therapeutic targets.

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.

Cyclopentapeptides from Dianthus chinensis

Han, Jing,Huang, Maobo,Wang, Zhe,Zheng, Yuqing,Zeng, Guangzhi,He, Wenjun,Tan, Ninghua

, p. 550 - 553 (2015)

A new cyclopentapeptide dianthin I (1), together with two known ones pseudostellarin A (2) and heterophyllin J (3), was isolated from the aerial parts of Dianthus chinensis. The structure of 1 was elucidated as cyclo-(Gly1- l-Phe2- l-Pro3- l-Ser4- l-Phe5) on the basis of extensive spectroscopic analyses and chemical methods.

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.

Structure of the Antifungal Nucleotide Antibiotic Phosmidosine

Phillips, Dennis R.,Uramoto, Masakazu,Isono, Kiyoshi,McCloskey, James A.

, p. 854 - 859 (1993)

The structure of phosmidosine (1), a novel proline-containing nucleotide antibiotic from Streptomyces durhameusis, active against the pathogenic fungus Botrytis cinerea, was determined by mass spectrometry and NMR spectroscopy.Homologs 2, 3, and the isomer 4 were detected and characterized using approaches based principally on tandem mass spectrometry and combined liquid chromatography-mass spectrometry which permitted assignment of most structural features directly in the crude isolate without prior isolation of individual components.Conversion of 1-4 to the O-isopropylidene derivatives 1a-4a by a microscale procedure resulted in enhanced fast atom bombardment ionization (FAB) signal to background sensitivity.Collision-induced dissociation mass spectra were aquired from molecular ions and ion source-generated fragment ions and used in conjunction with FAB-deuterium exchange methods for the assignment of structural differences between 1a-4a.

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.

Kinetics and mechanism of oxidation of captopril by diperiodatocuprate(III) in aqueous alkaline medium

Angadi, Mahantesh A.,Tuwar, Suresh M.

, p. 219 - 229 (2015)

Captopril is a sulfur containing drug which inhibits angiotensin-converting enzyme. Its kinetics of oxidation were studied spectrophotometrically using diperiodatocuprate(III) in aqueous alkali. Major oxidative product of captopril was identified as captopril disulfide along with trace amount of the hydrolyzed product, l-proline. Kinetics of oxidation was found to be first order each in [oxidant] and [reductant]. Rate of reaction was decreased by increasing [OH-], whereas added periodate retarded the rate. Other kinetic parameters viz., ionic strength, dielectric constant, temperature effect, and intervention of free radical were also studied. Activation parameters like EA, ΔH#, ΔS#, ΔG #, and log A were calculated. A suitable mechanism was proposed. Rate law for proposed mechanism was derived and verified. Reaction constants involved in various steps of mechanism were evaluated and used to regenerate first-order experimental rate constants at various experimental conditions.

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.

Enantioselective Enzymatic Cleavage of N-Benzyloxycarbonyl Groups

Patel, Ramesh N.,Nanduri, Venkata,Brzozowski, David,McNamee, Clyde,Banerjee, Amit

, p. 830 - 834 (2003)

A new enzymatic process for the enantioselective cleavage of N-benzyloxycarbonyl (Cbz) groups from protected amino acids and related compounds has been developed. The Cbz-deprotecting enzyme was isolated from cell extracts of Sphingomonas paucimobilis SC 16113 and purified to homogeneity. The purified protein has a molecular weight of 155,000 daltons and a subunit size of 44,000 daltons.

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