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D-Cysteine is an amino acid that plays a crucial role in various biological processes and has potential applications in different industries due to its unique properties.

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  • 921-01-7 Structure
  • Basic information

    1. Product Name: D-Cysteine
    2. Synonyms: D-Cysteine >=99% (RT);D-Cysteine, 98%, 98%;H-D-CYS-OH;D-CYS-OH;D-CYSTEINE;BETA-MERCAPTOALANINE;(S)-2-AMINO-3-MERCAPTOPROPIONIC ACID;RARECHEM AB PP 1441
    3. CAS NO:921-01-7
    4. Molecular Formula: C3H7NO2S
    5. Molecular Weight: 121.16
    6. EINECS: 213-062-0
    7. Product Categories: Amino Acids
    8. Mol File: 921-01-7.mol
  • Chemical Properties

    1. Melting Point: ~230 °C
    2. Boiling Point: 293.9 °C at 760 mmHg
    3. Flash Point: 131.5 °C
    4. Appearance: White/Crystalline Powder
    5. Density: 1.335 g/cm3
    6. Vapor Pressure: 0.000411mmHg at 25°C
    7. Refractive Index: 1.549
    8. Storage Temp.: −20°C
    9. Solubility: Aqueous Acid (Slightly), Water (Slightly)
    10. PKA: 2.07±0.10(Predicted)
    11. Water Solubility: Soluble in water (partly).
    12. Sensitive: Air Sensitive
    13. Stability: Stable. Incompatible with strong oxidizing agents.
    14. BRN: 1721407
    15. CAS DataBase Reference: D-Cysteine(CAS DataBase Reference)
    16. NIST Chemistry Reference: D-Cysteine(921-01-7)
    17. EPA Substance Registry System: D-Cysteine(921-01-7)
  • Safety Data

    1. Hazard Codes: Xi,Xn
    2. Statements: 36/37/38-20/21/22-22
    3. Safety Statements: 26-36-37/39-22
    4. WGK Germany: 3
    5. RTECS:
    6. F: 10-23
    7. HazardClass: N/A
    8. PackingGroup: N/A
    9. Hazardous Substances Data: 921-01-7(Hazardous Substances Data)

921-01-7 Usage

Uses

Used in Photocatalysis:
D-Cysteine is used as a functionalizing agent for quantum dots (QDs) to enhance their photocatalytic properties, making them more efficient in various photocatalytic applications.
Used in Carbon Dots Synthesis:
D-Cysteine is used as a precursor in the synthesis of cysteine-based chiral carbon dots (CDs), which have potential applications in various fields such as sensing, imaging, and drug delivery.
Used in Bioluminescence:
D-Cysteine is used in the synthesis of D-luciferin and aminoluciferin analogs, which are essential components in bioluminescent systems. These analogs can be used in various applications, including bioimaging, diagnostics, and as markers in biological research.

Check Digit Verification of cas no

The CAS Registry Mumber 921-01-7 includes 6 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 3 digits, 9,2 and 1 respectively; the second part has 2 digits, 0 and 1 respectively.
Calculate Digit Verification of CAS Registry Number 921-01:
(5*9)+(4*2)+(3*1)+(2*0)+(1*1)=57
57 % 10 = 7
So 921-01-7 is a valid CAS Registry Number.
InChI:InChI=1/C3H7NO2S/c4-2(1-7)3(5)6/h2,7H,1,4H2,(H,5,6)/t2-/m1/s1

921-01-7 Well-known Company Product Price

  • Brand
  • (Code)Product description
  • CAS number
  • Packaging
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  • Detail
  • Alfa Aesar

  • (H62627)  D-Cysteine, 98%   

  • 921-01-7

  • 1g

  • 488.0CNY

  • Detail
  • Alfa Aesar

  • (H62627)  D-Cysteine, 98%   

  • 921-01-7

  • 5g

  • 2197.0CNY

  • Detail
  • Aldrich

  • (30095)  D-Cysteine  ≥99% (RT)

  • 921-01-7

  • 30095-100MG

  • 647.01CNY

  • Detail
  • Aldrich

  • (30095)  D-Cysteine  ≥99% (RT)

  • 921-01-7

  • 30095-1G

  • 3,231.54CNY

  • Detail

921-01-7SDS

SAFETY DATA SHEETS

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

Version: 1.0

Creation Date: Aug 17, 2017

Revision Date: Aug 17, 2017

1.Identification

1.1 GHS Product identifier

Product name D-cysteine

1.2 Other means of identification

Product number -
Other names (S)-2-amino-3-mercaptopropanoic acid

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
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:921-01-7 SDS

921-01-7Synthetic route

Conditions
ConditionsYield
With hydroxylamine hydrochloride83%
With hydroxylamine hydrochloride In methanol reflux, 120 min, ice bath, 60 min;82%
(2S,4S)-2-(D-galacto-1,2,3,4,5-Pentahydroxypentyl)-4-thiazolidincarbonsaeure
88271-26-5

(2S,4S)-2-(D-galacto-1,2,3,4,5-Pentahydroxypentyl)-4-thiazolidincarbonsaeure

D-cysteine
921-01-7

D-cysteine

Conditions
ConditionsYield
With hydroxylamine hydrochloride In methanol for 2h; Heating;73%
Conditions
ConditionsYield
With hydroxylamine hydrochloride In methanol; water for 3.5h; Heating;60%
Conditions
ConditionsYield
beim selektiven Abbau durch Escherichia coli;
S,S-cystine
349-46-2

S,S-cystine

D-cysteine
921-01-7

D-cysteine

Conditions
ConditionsYield
With hydrogenchloride; tin
(D)-2-Amino-3-(benzylthio)propanoic acid
3054-01-1, 5680-65-9, 16597-46-9, 23032-53-3

(D)-2-Amino-3-(benzylthio)propanoic acid

D-cysteine
921-01-7

D-cysteine

Conditions
ConditionsYield
With ammonia; sodium
(2R,2'R)-2-amino-4-(2'-amino-2'-carboxyethylsulfanyl)butanoic acid
2998-83-6

(2R,2'R)-2-amino-4-(2'-amino-2'-carboxyethylsulfanyl)butanoic acid

D-cysteine
921-01-7

D-cysteine

Conditions
ConditionsYield
Spaltung durch Leber-Extrakt;
L-Cysteine
52-90-4

L-Cysteine

D-cysteine
921-01-7

D-cysteine

Conditions
ConditionsYield
With water; acetone Product distribution; 1.) acetic acid, reflux, 2.5 h; 2.) methanol, room temp, 30 min;
3-chloro-DL-alanine
3981-36-0

3-chloro-DL-alanine

D-cysteine
921-01-7

D-cysteine

Conditions
ConditionsYield
With sodium hydrogensulfide; potassium phosphate buffer; acetone at 30℃; for 2h; 3-chloro-D-alanine-lyase; Yield given;
Conditions
ConditionsYield
With dinitrogen sulphide; pyridoxal 5'-phosphate; sodium dodecyl-sulfate at 30℃; for 3.5h; Pseudomonas fluorescens CR 19-1, 0.1 M phosphate buffer, pH 8.5;
With sodium hydrogensulfide; potassium phosphate buffer; pyridoxal 5'-phosphate In acetone at 30℃; for 2h; Pseudomonas putida CR 1-1 cells; Yield given;
4-ethylbenzenesulfonic acid D-cysteine salt

4-ethylbenzenesulfonic acid D-cysteine salt

D-cysteine
921-01-7

D-cysteine

Conditions
ConditionsYield
With triethylamine In methanol for 0.5h;
Conditions
ConditionsYield
With teicoplanin In methanol; water Product distribution; Further Variations:; Reagents; pH-values; Solvents;
Resolution of racemate; enantioselective reaction;A n/a
B n/a
Resolution of racemate; enantioselective reaction;A n/a
B n/a
With R-(3,3'-dibromo-1,1'-binaphthyl)-20-crown-6 coated C18 silica gel column at 25℃; pH=2; Resolution of racemate;
With capillary electrochromatography open-tubular column coated with 1-allylimidazolium-β-cyclodextrin In aq. acetate buffer at 20℃; pH=8; pH-value; Resolution of racemate;
hydrgensulfide(1-)

hydrgensulfide(1-)

L-cystine
6020-39-9

L-cystine

A

D-cysteine
921-01-7

D-cysteine

B

disulfide

disulfide

Conditions
ConditionsYield
In further solvent(s) Kinetics; in pH 10.0 borate buffer; detected with UV-vis sectroscopy and ion-exchange chromatography;
hapalocyclamide
1359827-55-6

hapalocyclamide

A

L-alanin
56-41-7

L-alanin

B

D-Alanine
338-69-2

D-Alanine

C

D-cysteine
921-01-7

D-cysteine

D

Phenylalanine
150-30-1

Phenylalanine

Conditions
ConditionsYield
With hydrogenchloride; water at 100℃; for 19h;
hapalocyclamide
1359827-55-6

hapalocyclamide

A

D-Alanine
338-69-2

D-Alanine

B

D-cysteine
921-01-7

D-cysteine

C

L-phenylalanine
63-91-2

L-phenylalanine

D

D-(R)-phenylalanine
673-06-3

D-(R)-phenylalanine

Conditions
ConditionsYield
With hydrogenchloride; water at 100℃; for 1h;
Z-Ile-Glu(OMe)-Thr-Asp(OMe)-D-Cys

Z-Ile-Glu(OMe)-Thr-Asp(OMe)-D-Cys

D-cysteine
921-01-7

D-cysteine

Conditions
ConditionsYield
With caspase 8 for 1h;
D-cysteine
921-01-7

D-cysteine

2,4-Di-tert-butoxy-pyrimidine-5-carbaldehyde
172949-72-3

2,4-Di-tert-butoxy-pyrimidine-5-carbaldehyde

(2S,4S)-2-(2,4-Di-tert-butoxy-pyrimidin-5-yl)-thiazolidine-4-carboxylic acid
1025823-01-1

(2S,4S)-2-(2,4-Di-tert-butoxy-pyrimidin-5-yl)-thiazolidine-4-carboxylic acid

Conditions
ConditionsYield
In ethanol; water100%
D-cysteine
921-01-7

D-cysteine

propyl bromide
106-94-5

propyl bromide

S-propyl-D-cysteine
85955-34-6

S-propyl-D-cysteine

Conditions
ConditionsYield
With ammonia; sodium98%
D-cysteine
921-01-7

D-cysteine

allyl alcohol
107-18-6

allyl alcohol

Fudosteine

Fudosteine

Conditions
ConditionsYield
With potassium sulfate In water at 30℃;98%
D-cysteine
921-01-7

D-cysteine

tert-butyl 4-iodobutanoate
6182-78-1

tert-butyl 4-iodobutanoate

4-((2S)-amino-2-carboxy-ethylsulfanyl)-butyric acid tert-butyl ester

4-((2S)-amino-2-carboxy-ethylsulfanyl)-butyric acid tert-butyl ester

Conditions
ConditionsYield
Stage #1: D-cysteine With sodium hydroxide; water In methanol at 0℃;
Stage #2: tert-butyl 4-iodobutanoate In methanol for 0.0833333h;
Stage #3: With hydrogenchloride; water In methanol pH=~ 8;
97%
D-cysteine
921-01-7

D-cysteine

2-cyano-6-hydroxybenzothiazole
939-69-5

2-cyano-6-hydroxybenzothiazole

D-luciferin
2591-17-5

D-luciferin

Conditions
ConditionsYield
In water at 20℃;95%
With ammonia; sodium In methanol; water94%
Stage #1: D-cysteine; 2-cyano-6-hydroxybenzothiazole In aq. buffer for 1h;
Stage #2: With ATP; magnesium chloride; zinc(II) chloride; luciferase In aq. buffer
27%
methanol
67-56-1

methanol

D-cysteine
921-01-7

D-cysteine

D-cysteine methyl ester hydrochloride
5714-80-7, 18598-63-5, 70361-61-4

D-cysteine methyl ester hydrochloride

Conditions
ConditionsYield
With acetyl chloride at 0℃; for 2h; Reflux;94%
With hydrogenchloride for 12h;
With hydrogenchloride at 100℃; for 0.5h;
ethyleneimine
151-56-4

ethyleneimine

D-cysteine
921-01-7

D-cysteine

2-amino-3-<(2-aminoethyl)thio>-propanoic acid
53526-71-9

2-amino-3-<(2-aminoethyl)thio>-propanoic acid

Conditions
ConditionsYield
With phosphate buffer at 0℃; pH 8.0;92%
D-cysteine
921-01-7

D-cysteine

mono-4-methoxytrityl chloride
14470-28-1

mono-4-methoxytrityl chloride

C23H23NO3S
926935-33-3

C23H23NO3S

Conditions
ConditionsYield
In N,N-dimethyl-formamide at 20℃; for 48h; Inert atmosphere;92%
6-(methylamino)benzo[d]-thiazole-2-carbonitrile
934270-86-7

6-(methylamino)benzo[d]-thiazole-2-carbonitrile

D-cysteine
921-01-7

D-cysteine

D-(-)-2-(6'-methylamino-2'-benzothiazolyl)-Δ2-thiazoline-4-carboxylic acid

D-(-)-2-(6'-methylamino-2'-benzothiazolyl)-Δ2-thiazoline-4-carboxylic acid

Conditions
ConditionsYield
In methanol for 1h; pH=8; aq. sodium phosphate buffer; Inert atmosphere;91%
D-cysteine
921-01-7

D-cysteine

2-Hydroxy-3-methoxybenzonitrile
6812-16-4

2-Hydroxy-3-methoxybenzonitrile

(S)-2-(2-Hydroxy-3-methoxy-phenyl)-4,5-dihydro-thiazole-4-carboxylic acid

(S)-2-(2-Hydroxy-3-methoxy-phenyl)-4,5-dihydro-thiazole-4-carboxylic acid

Conditions
ConditionsYield
With phosphate buffer In methanol at 70℃; for 17h;90%
methanol
67-56-1

methanol

D-cysteine
921-01-7

D-cysteine

(S)-(+)-Cysteinmethylester

(S)-(+)-Cysteinmethylester

Conditions
ConditionsYield
Stage #1: methanol With acetyl chloride at 0℃; for 0.0833333h;
Stage #2: D-cysteine for 6h; Reflux;
90%
D-cysteine
921-01-7

D-cysteine

di-tert-butyl dicarbonate
24424-99-5

di-tert-butyl dicarbonate

N,N’-di-Boc-L-cystine
126686-73-5

N,N’-di-Boc-L-cystine

Conditions
ConditionsYield
With sodium hydroxide In tetrahydrofuran; water for 24h; pH=10;89%
D-cysteine
921-01-7

D-cysteine

6-((4-(dimethylamino)phenyl)amino)benzo[d]thiazole-2-carbonitrile

6-((4-(dimethylamino)phenyl)amino)benzo[d]thiazole-2-carbonitrile

(S)-2-(6-((4-(dimethylamino)phenyl)amino)benzo[d]thiazol-2-yl)-4,5-dihydrothiazole-4-carboxylic acid

(S)-2-(6-((4-(dimethylamino)phenyl)amino)benzo[d]thiazol-2-yl)-4,5-dihydrothiazole-4-carboxylic acid

Conditions
ConditionsYield
In methanol; aq. phosphate buffer for 1h; pH=8; Inert atmosphere;88%
ethanol
64-17-5

ethanol

D-cysteine
921-01-7

D-cysteine

D-cysteine ethyl ester hydrochloride
75521-14-1

D-cysteine ethyl ester hydrochloride

Conditions
ConditionsYield
Stage #1: ethanol With thionyl chloride at -5 - 20℃; for 1.5h;
Stage #2: D-cysteine at 50℃; for 4h;
87.5%
D-cysteine
921-01-7

D-cysteine

2,4-Dimethoxybenzaldehyde
613-45-6

2,4-Dimethoxybenzaldehyde

C12H15NO4S

C12H15NO4S

Conditions
ConditionsYield
In ethanol at 20℃; for 48h;87%
D-cysteine
921-01-7

D-cysteine

N-(2-cyanobenzo[d]thiazol-6-yl)ethanesulfonamide

N-(2-cyanobenzo[d]thiazol-6-yl)ethanesulfonamide

(S)-2-(6-(ethylsulfonamido)benzo[d]thiazol-2-yl)-4,5-dihydrothiazole-4-carboxylic acid

(S)-2-(6-(ethylsulfonamido)benzo[d]thiazol-2-yl)-4,5-dihydrothiazole-4-carboxylic acid

Conditions
ConditionsYield
In methanol; aq. phosphate buffer for 1h; pH=8;86%
D-cysteine
921-01-7

D-cysteine

N-(2-cyanobenzo[d]thiazol-6-yl)methanesulfonamide

N-(2-cyanobenzo[d]thiazol-6-yl)methanesulfonamide

(S)-2-(6-(methylsulfonamido)benzo[d]thiazol-2-yl)-4,5-dihydrothiazole-4-carboxylic acid

(S)-2-(6-(methylsulfonamido)benzo[d]thiazol-2-yl)-4,5-dihydrothiazole-4-carboxylic acid

Conditions
ConditionsYield
In aq. phosphate buffer; acetonitrile for 1h; pH=8;86%
D-cysteine
921-01-7

D-cysteine

benzyl chloroformate
501-53-1

benzyl chloroformate

methyl iodide
74-88-4

methyl iodide

N-(benzyloxycarbonyl)-S-methyl-D-cysteine
95406-98-7

N-(benzyloxycarbonyl)-S-methyl-D-cysteine

Conditions
ConditionsYield
Stage #1: D-cysteine; methyl iodide With sodium In methanol
Stage #2: benzyl chloroformate With sodium hydroxide
85%
diethyl sulfate
64-67-5

diethyl sulfate

D-cysteine
921-01-7

D-cysteine

(S)-2-amino-3-(ethylthio)propanoic acid

(S)-2-amino-3-(ethylthio)propanoic acid

Conditions
ConditionsYield
With barium(II) hydroxide at 20℃; for 3h;85%
D-cysteine
921-01-7

D-cysteine

(4-hydroxyphenyl)methanol
623-05-2

(4-hydroxyphenyl)methanol

D-[S-(4'-hydroxybenzyl)]cysteine

D-[S-(4'-hydroxybenzyl)]cysteine

Conditions
ConditionsYield
With hydrogenchloride In water at 20℃; for 0.333333h; pH=2;84.7%
D-cysteine
921-01-7

D-cysteine

6-((4-hydroxyphenyl)amino)benzo[d]thiazole-2-carbonitrile

6-((4-hydroxyphenyl)amino)benzo[d]thiazole-2-carbonitrile

(S)-2-(6-((4-hydroxyphenyl)amino)benzo[d]thiazol-2-yl)-4,5-dihydrothiazole-4-carboxylic acid

(S)-2-(6-((4-hydroxyphenyl)amino)benzo[d]thiazol-2-yl)-4,5-dihydrothiazole-4-carboxylic acid

Conditions
ConditionsYield
In methanol; aq. phosphate buffer for 1h; pH=8; Inert atmosphere;84%
D-cysteine
921-01-7

D-cysteine

6-(2-oxooxazolidin-3-yl)benzo[d]thiazole-2-carbonitrile

6-(2-oxooxazolidin-3-yl)benzo[d]thiazole-2-carbonitrile

(S)-2-(6-(2-oxooxazolidin-3-yl)benzo[d]thiazol-2-yl)-4,5-dihydrothiazole-4-carboxylic acid

(S)-2-(6-(2-oxooxazolidin-3-yl)benzo[d]thiazol-2-yl)-4,5-dihydrothiazole-4-carboxylic acid

Conditions
ConditionsYield
In methanol; aq. phosphate buffer for 1h; pH=8; Inert atmosphere;84%
D-cysteine
921-01-7

D-cysteine

5-methoxythiazolo[5,4-b]pyridine-2-carbonitrile
1417816-65-9

5-methoxythiazolo[5,4-b]pyridine-2-carbonitrile

(S)-2-(5-methoxy-thiazolo[5,4-b]pyridin-2-yl)-4,5-dihydrothiazole-4-carboxylic acid

(S)-2-(5-methoxy-thiazolo[5,4-b]pyridin-2-yl)-4,5-dihydrothiazole-4-carboxylic acid

Conditions
ConditionsYield
With potassium carbonate In water; N,N-dimethyl-formamide; acetonitrile for 0.166667h;83%
D-cysteine
921-01-7

D-cysteine

6-fluorobenzo[d]thiazole-2-carbonitrile
169776-04-9

6-fluorobenzo[d]thiazole-2-carbonitrile

(S)-2-(6-fluorobenzo[d]thiazol-2-yl)-4,5-dihydrothiazole-4-carboxylic acid

(S)-2-(6-fluorobenzo[d]thiazol-2-yl)-4,5-dihydrothiazole-4-carboxylic acid

Conditions
ConditionsYield
In methanol; aq. phosphate buffer for 1h; pH=8; Inert atmosphere;81%
D-cysteine
921-01-7

D-cysteine

N-(2-cyanobenzo[d]thiazol-6-yl)cyclopentanesulfonamide

N-(2-cyanobenzo[d]thiazol-6-yl)cyclopentanesulfonamide

(S)-2-(6-(cyclopentanesulfonamido)benzo[d]thiazol-2-yl)-4,5-dihydrothiazole-4-carboxylic acid

(S)-2-(6-(cyclopentanesulfonamido)benzo[d]thiazol-2-yl)-4,5-dihydrothiazole-4-carboxylic acid

Conditions
ConditionsYield
In methanol; aq. phosphate buffer for 1h; pH=8;80%
D-cysteine
921-01-7

D-cysteine

2-cyanobenzo[d]thiazol-6-yl 4-oxopentanoate

2-cyanobenzo[d]thiazol-6-yl 4-oxopentanoate

(S)-2-(6-((4-oxopentanoyl)oxy)benzo[d]thiazol-2-yl)-4,5-dihydrothiazole-4-carboxylic acid

(S)-2-(6-((4-oxopentanoyl)oxy)benzo[d]thiazol-2-yl)-4,5-dihydrothiazole-4-carboxylic acid

Conditions
ConditionsYield
In methanol; dichloromethane; water at 0 - 25℃; for 0.5h; Inert atmosphere;79.7%
D-cysteine
921-01-7

D-cysteine

N-(2-cyanobenzo[d]thiazol-6-yl)propane-2-sulfonamide

N-(2-cyanobenzo[d]thiazol-6-yl)propane-2-sulfonamide

(S)-2-(6-(1-methylethylsulfonamido)benzo[d]thiazol-2-yl)-4,5-dihydrothiazole-4-carboxylic acid

(S)-2-(6-(1-methylethylsulfonamido)benzo[d]thiazol-2-yl)-4,5-dihydrothiazole-4-carboxylic acid

Conditions
ConditionsYield
In methanol; aq. phosphate buffer for 1h; pH=8;79%
1-(3',4'-dihydroxyphenyl)decan-3-one

1-(3',4'-dihydroxyphenyl)decan-3-one

D-cysteine
921-01-7

D-cysteine

3’-S-cysteinyl-1-(3,4-dihydroxyphenyl)decan-3-one

3’-S-cysteinyl-1-(3,4-dihydroxyphenyl)decan-3-one

Conditions
ConditionsYield
With 1-hydroxy-3H-benz[d][1,2]iodoxole-1,3-dione In methanol; aq. phosphate buffer at -78 - 20℃; for 1.5h;78%

921-01-7Relevant articles and documents

MODIFIED INTERLEUKIN-7 PROTEINS AND USES THEREOF

-

, (2021/10/22)

Provided are a modified IL-7 polypeptide and a fusion protein containing the modified IL-7 polypeptide. The fusion protein of the modified IL-7 includes: a first domain containing an interleukin-7 polypeptide; a second domain containing an oligopeptide having 1 to 10 amino acid residues (with proviso that the second domain excludes the oligopeptide consisting of methionine and/or glycine); and (c) a third domain which prolongs the half-life of the IL-7 fusion protein. The modified IL-7 polypeptide is composed of the (a) first domain and the (b) second domain. The modified IL-7 polypeptide and the fusion protein are expressed in a higher yield than the wild-type IL-7 and shows increased stability.

Synthesis method of DL-cysteine

-

Paragraph 0020-0022, (2021/02/13)

The invention discloses a synthetic method of DLcysteine. The method comprises the following steps: by using acrylonitrile as a raw material, chlorinating to generate 2, 3dichloropropionitrile, hydrolyzing to generate corresponding acid, reacting the acid with thiourea to cyclize to generate 2-aminothiazoline-4-carboxylic acid, adding alkali sulfide to generate 2-mercaptothiazoline-4-carboxylic acid, and hydrolyzing to generate cysteine. The synthesis method provided by the invention has the advantages of short synthesis steps, mild preparation conditions, sufficient and cheap raw material sources and higher product yield.

Cysteine Chemistry in Connection with Abiogenesis

Bridoux, Maxime,Ceccarelli, Cecilia,Shalayel, Ibrahim,Vallée, Yannick,Vazart, Fanny,Youssef-Saliba, Sparta

supporting information, (2020/05/18)

Theoretical and experimental work has been conducted about possible prebiotic syntheses of cysteine. Activated derivatives of this amino acid can oligomerize and polymerize to afford various poly-thiazolines and cysteine-rich chains.

Preparation and characterization of a new open-tubular capillary column for enantioseparation by capillary electrochromatography

Li, Yingjie,Tang, Yimin,Qin, Shili,Li, Xue,Dai, Qiang,Gao, Lidi

, p. 283 - 292 (2019/02/05)

In order to use the enantioseparation capability of cationic cyclodextrin and to combine the advantages of capillary electrochromatography (CEC) with open-tubular (OT) column, in this study, a new OT-CEC, coated with cationic cyclodextrin (1-allylimidazolium-β-cyclodextrin [AI-β-CD]) as chiral stationary phase (CSP), was prepared and applied for enantioseparation. Synthesized AI-β-CD was characterized by infrared (IR) spectrometry and mass spectrometry (MS). The preparation conditions for the AI-β-CD-coated column were optimized with the orthogonal experiment design L9(34). The column prepared was characterized by scanning electron microscopy (SEM) and elemental analysis (EA). The results showed that the thickness of stationary phase in the inner surface of the AI-β-CD-coated columns was about 0.2 to 0.5?μm. The AI-β-CD content in stationary phase based on the EA was approximately 2.77?mmol·m?2. The AI-β-CD-coated columns could separate all 14 chiral compounds (histidine, lysine, arginine, glutamate, aspartic acid, cysteine, serine, valine, isoleucine, phenylalanine, salbutamol, atenolol, ibuprofen, and napropamide) successfully in the study and exhibit excellent reproducibility and stability. We propose that the column, coated with AI-β-CD, has a great potential for enantioseparation in OT-CEC.

Dynamic Kinetic Resolution for Asymmetric Synthesis of L-Noncanonical Amino Acids from D-Ser Using Tryptophan Synthase and Alanine Racemase

Yu, Jinhai,Li, Jing,Gao, Xia,Zeng, Shuiyun,Zhang, Hongjuan,Liu, Junzhong,Jiao, Qingcai

, p. 6618 - 6625 (2019/11/03)

L-Ser is often used to synthesize some significant l-noncanonical α-amino acids(l-ncAAs), which are the prevalent intermediates and precursors for functional synthetic compounds. In this study, threonine aldolase from Escherichia coli k-12 MG1655 has been used to synthesize l-Ser. In contrast to the maximum catalytic capacity (20 g/L) for l-threonine aldolase(LTA), d-Ser was synthesized with high yield (240 g/L) from cheap Gly and paraformaldehyde using d-threonine aldolase (DTA) from Arthrobacter sp ATCC. In order to fully utilize d-Ser and expand the resource of l-Ser, a dynamic kinetic resolution system was constructed to convert d/dl-Ser to l-Ser through combining alanine racemase (Alr) from Bacillus subtilis with l-tryptophan synthase (TrpS) from Escherichia coli k-12 MG1655, and l-ncAAs including l-Trp and l-Cys derivatives were synthesized with excellent enantioselectivity and in high yields. The results indicated l-ncAAs could be efficiently synthesized from d-Ser using this original and green dynamic kinetic resolution system, and the reliable l-Ser resource has been established from simple and achiral substrates.

T Cells with Increased Immunosuppression Resistance

-

, (2018/02/06)

This invention relates to the treatment of cancer in an individual by administration of a population of modified T cells that express a recombinant cAMP phosphodiesterase (PDE) or a fragment thereof and an antigen receptor which binds specifically to cancer cells in the individual. Populations of modified T cells and methods of producing populations of modified T cells are provided, along with pharmaceutical compositions and methods of treatment

Chromatographic Resolution of α-Amino Acids by (R)-(3,3'-Halogen Substituted-1,1'-binaphthyl)-20-crown-6 Stationary Phase in HPLC

Wu, Peng,Wu, Yuping,Zhang, Junhui,Lu, Zhenyu,Zhang, Mei,Chen, Xuexian,Yuan, Liming

supporting information, p. 1037 - 1042 (2017/07/25)

Three new chiral stationary phases (CSPs) for high-performance liquid chromatography were prepared from R-(3,3'-halogen substituted-1,1'-binaphthyl)-20-crown-6 (halogen = Cl, Br and I). The experimental results showed that R-(3,3'-dibromo-1,1'-binaphthyl)-20-crown-6 (CSP-1) possesses more prominent enantioselectivity than the two other halogen-substituted crown ether derivatives. All twenty-one α-amino acids have different degrees of separation on R-(3,3'-dibromo-1,1'-binaphthyl)-20-crown-6-based CSP-1 at room temperature. The enantioselectivity of CSP-1 is also better than those of some commercial R-(1,1'-binaphthyl)-20-crown-6 derivatives. Both the separation factors (α) and the resolution (Rs) are better than those of commercial crown ether-based CSPs [CROWNPAK CR(+) from Daicel] under the same conditions for asparagine, threonine, proline, arginine, serine, histidine and valine, which cannot be separated by commercial CR(+). This study proves the commercial usefulness of the R-(3,3'-dibromo-1,1'-binaphthyl)-20-crown-6 chiral stationary phase.

Protection of Endogenous Thiols against Methylmercury with Benzimidazole-Based Thione by Unusual Ligand-Exchange Reactions

Banerjee, Mainak,Karri, Ramesh,Chalana, Ashish,Das, Ranajit,Rai, Rakesh Kumar,Rawat, Kuber Singh,Pathak, Biswarup,Roy, Gouriprasanna

supporting information, p. 5696 - 5707 (2017/04/28)

Organomercurials, such as methylmercury (MeHg+), are among the most toxic materials to humans. Apart from inhibiting proteins, MeHg+ exerts its cytotoxicity through strong binding with endogenous thiols cysteine (CysH) and glutathione (GSH) to form MeHgCys and MeHgSG complexes. Herein, it is reported that the N,N-disubstituted benzimidazole-based thione 1 containing a N?CH2CH2OH substituent converts MeHgCys and MeHgSG complexes to less toxic water-soluble HgS nanoparticles (NPs) and releases the corresponding free thiols CysH and GSH from MeHgCys and MeHgSG, respectively, in solution by unusual ligand-exchange reactions in phosphate buffer at 37 °C. However, the corresponding N-substituted benzimidazole-based thione 7 and N,N-disubstituted imidazole-based thione 3, in spite of containing a N?CH2CH2OH substituent, failed to convert MeHgX (X=Cys, and SG) to HgS NPs under identical reaction conditions, which suggests that not only the N?CH2CH2OH moiety but the benzimidazole ring and N,N-disubstitution in 1, which leads to the generation of a partial positive charge at the C2 atom of the benzimidazole ring in 1:1 MeHg-conjugated complex of 1, are crucial to convert MeHgX to HgS NPs under physiologically relevant conditions.

(-)/(+)-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 (2016/06/14)

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

Reaction of hydrogen sulfide with disulfide and Sulfenic acid to form the strongly Nucleophilic Persulfide

Cuevasanta, Ernesto,Lange, Mike,Bonanata, Jenner,Coiti?o, E. Laura,Ferrer-Sueta, Gerardo,Filipovic, Milos R.,Alvarez, Beatriz

, p. 26866 - 26880 (2015/11/17)

Background: Hydrogen sulfide (H2S) modulates physiological processes in mammals. Results: The reactivity of H2S toward disulfides (RSSR) and albumin sulfenic acid (RSOH) to form persulfides (RSSH) was assessed. Conclusion: H2S is less reactive than thiols. Persulfides have enhanced nucleophilicity. Significance: This kinetic study helps rationalize the contribution of the reactions with oxidized thiol derivatives toH2S biology.

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