147857-42-9

Basic information

• Product Name: methyl (2R)-2-amino-4-{[(3S)-3-amino-4-methoxy-4-oxobutyl]disulfanyl}butanoate dihydrochloride
• CAS NO: 147857-42-9
• Molecular Weight: 369.334
• Mol File: 147857-42-9.mol

Chemical Properties

• CAS DataBase Reference: methyl (2R)-2-amino-4-{[(3S)-3-amino-4-methoxy-4-oxobutyl]disulfanyl}butanoate dihydrochloride(CAS DataBase Reference)
• NIST Chemistry Reference: methyl (2R)-2-amino-4-{[(3S)-3-amino-4-methoxy-4-oxobutyl]disulfanyl}butanoate dihydrochloride(147857-42-9)
• EPA Substance Registry System: methyl (2R)-2-amino-4-{[(3S)-3-amino-4-methoxy-4-oxobutyl]disulfanyl}butanoate dihydrochloride(147857-42-9)

Safety Data

• Hazardous Substances Data: 147857-42-9(Hazardous Substances Data)

Upstream product

• 67-56-1 methanol 
• 462-10-2 DL-homocystine 
• 626-72-2 L-homocystine 
• 7093-69-8 4,4'-disulfanediylbis(2-aminobutanoic acid) 
• 6027-13-0 L-homocysteine 
• 130981-51-0 (2S,2'S)-4,4'-disulfanediylbis(2-(tert-butoxycarbonyl)amino)butanoic acid 

Relevant articles and documents

CRYSTALLINE SULFAMIDE COMPOUND

The present application relates to a crystalline sulfamide compound, and in particular relates to a crystalline (S)-N-((S)-1-(2-chlorphenyl)-2-((3,3-difluorocyclobutyl)amido)-2oxoethyl)-2-(4-cyanopyridin-2-base)-N-(3-fluorophenyl)-isothiazolidine-3-formam

SULTAM COMPOUND AND APPLICATION METHOD THEREOF

Provided are a sultam compound having isocitrate dehydrogenase 1 (IDH1) inhibitory activity as represented by formula I or pharmaceutically-acceptable salts, solvates or hydrates thereof, a preparation method thereof, and a pharmaceutical composition containing the compound. The compound or the pharmaceutically-acceptable salts, solvates or hydrates thereof, and the pharmaceutical composition containing the compound can be used to treat IDH1 mutation-induced cancers.

COMPOUNDS AS L-CYSTINE CRYSTALLIZATION INHIBITORS AND USES THEREOF

A method of preventing or inhibiting L-cystine crystallization is disclosed, using the compounds of formula I: [in-line-formulae]R1a—[O]v-(-A-L-)m-A-[O]v—R1b [/in-line-formulae] wherein A, L, R1a, R1b, m, and v are as described herein. The compounds may be prepared as pharmaceutical compositions, and may be used for the prevention and treatment of conditions that are causally related to L-cystine crystallization, such as comprising (but not limited to) kidney stones.

A Sulfoxide-Based Isobaric Labelling Reagent for Accurate Quantitative Mass Spectrometry

Modern proteomics requires reagents for exact quantification of peptides in complex mixtures. Peptide labelling is most typically achieved with isobaric tags that consist of a balancer and a reporter part that separate in the gas phase. An ingenious distribution of stable isotopes provides multiple reagents with identical molecular weight but a different mass of the reporter groups, allowing relative quantification of multiple samples in one measurement. Here we report a new isobaric labelling reagent, where the balancer and the reporter are linked by a sulfoxide group, which, based on the sulfoxide pyrolysis, leads to easy and asymmetric cleavage at low fragmentation energy. The fragmentation of our new design is significantly improved, yielding more intense complementary ion signals, allowing complementary ion cluster analysis as well.

PEPTIDES AS OXYTOCIN AGONISTS

The present compounds are oxytocin receptor agonists for the treatment of autism, stress, including post-traumatic stress disorder, anxiety, including anxiety disorders and depression, schizophrenia, psychiatric disorders and memory loss, alcohol withdraw

Synthesis and evaluation of new ω-borono-α-amino acids as rat liver arginase inhibitors

Recent studies have demonstrated that arginase plays important roles in pathologies such as asthma or erectile dysfunctions. We have synthesized new ω-borono-α-amino acids that are analogues of the previously known arginase inhibitors S-(2-boronoethyl)-l-cysteine (BEC) and 2-amino-6- boronohexanoic acid (ABH) and evaluated them as inhibitors of purified rat liver arginase (RLA). In addition to the distance between the B(OH)2 and the α-amino acid functions, the position of the sulfur atom in the side chain also appears as a key determinant for the interaction with the active site of RLA. Furthermore, substitution of the alkyl side chain of BEC by methyl groups and conformational restriction of ABH by incorporation of its side chain in a phenyl ring led to inactive compounds. These results suggest that subtle interactions govern the affinity of inhibitors for the active site of RLA.

Probing the stereochemistry of the active site of gamma-glutamyl transpeptidase using sulfur derivatives of l-glutamic acid.

Gamma-glutamyl transpeptidase (GGT) catalyses the transfer of a gamma-glutamyl moiety from a donor substrate to different acceptors, such as amino acids and water. GGT is known to display relatively low stereospecificity with respect to the alpha-stereocentre of its donor substrates. In this study we have studied its stereospecificity with respect to the stereocentre at the delta-position of different analogues of L-glutamic acid. Notably, L-methionine sulfoxide is well-recognised whereas L-methionine sulfone and L-methionine sulfoximine are not. Furthermore, when the synthetic gamma-diastereoisomers of L-methionine sulfoxide were separated and tested, it was discovered that GGT shows remarkable stereospecificity at the gamma-position, binding the S(C)S(S) diastereoisomer with a K(i) of 3.5 mM, whereas the S(C)R(S) diastereoisomer is not recognised. Finally, using a sulfoxide as a new pharmacophore for GGT, we have synthesized and tested an analogue of glutathione to obtain a very promising competitive inhibitor with a K(i) of (53 +/- 3) microM.

Chemical synthesis of S-ribosyl-L-homocysteine and activity assay as a LuxS substrate

Bacterial quorum sensing is mediated by autoinducers, small signaling molecules generated by bacteria. It has been proposed that the LuxS enzyme converts S-ribosyl-L-homocysteine to 4,5-dihydroxy-2,3-pentanedione, the precursor of autoinducer 2 (AI-2). We report here a chemical synthesis of S-ribosyl-L-homocysteine and its analogue using Mitsunobu coupling. Chemically synthesized ribosylhomocysteine has been confirmed as a substrate for LuxS in both an enzyme assay and a whole cell quorum sensing assay. The chemical entities of products from the LuxS reaction were also established. Several ribosylhomocysteine analogues have been tested as LuxS inhibitors.

Synthesis and in vitro enzyme activity of aza, oxa and thia derivatives of bacterial cell wall biosynthesis intermediates

Mechanism based inhibitors of diaminopimelate aminotransferase (DAP-AT) were designed using knowledge of its substrate specificity and mechanism. Synthesis of thiolester and amide substrate analogues was achieved prior to in vitro inhibition studies, but ester analogues proved too unstable to isolate. Thia substrate analogues showed no inhibitory properties, but the aza substrate analogue 12a showed reversible inhibition vs. DAP-AT and time dependent inhibition in the absence of the natural substrate 4. Substrate analogue 12a is thefirst example of an amide inhibitor of PLP dependent enzymes. Antibiotic properties of 12a were also briefly assessed.