115364-77-7

Basic information

• Product Name: (R)-N-tert-butyloxycarbonyl-3-amino-4-phenyl-N'-(benzyloxy)-N'-methylbutanamide
• Synonyms: (R)-N-tert-butyloxycarbonyl-3-amino-4-phenyl-N'-(benzyloxy)-N'-methylbutanamide
• CAS NO: 115364-77-7
• Molecular Weight: 398.502
• Mol File: 115364-77-7.mol
• Article Data: 1

Chemical Properties

• CAS DataBase Reference: (R)-N-tert-butyloxycarbonyl-3-amino-4-phenyl-N'-(benzyloxy)-N'-methylbutanamide(CAS DataBase Reference)
• NIST Chemistry Reference: (R)-N-tert-butyloxycarbonyl-3-amino-4-phenyl-N'-(benzyloxy)-N'-methylbutanamide(115364-77-7)
• EPA Substance Registry System: (R)-N-tert-butyloxycarbonyl-3-amino-4-phenyl-N'-(benzyloxy)-N'-methylbutanamide(115364-77-7)

Safety Data

• Hazardous Substances Data: 115364-77-7(Hazardous Substances Data)

Upstream product

• 22513-22-0 N-methyl-O-benzylhydroxylamine 
• 101555-61-7 (R)-3-t-butoxycarbonylamino-4-phenylbutyric acid 
• 115313-19-4 1-diazo-3(R)-<<(1,1-dimethylethoxy)carbonyl>amino>-4-phenyl-2-butanone 

Downstream Products

• 115364-79-9 (R)-3-amino-4-phenyl-N'-(benzyloxy)-N'-methylbutanamide trifluoroacetate 

Relevant articles and documents

Retro-inverso concept applied to the complete inhibitors of enkephalin-degrading enzymes

Peptide retro-inverso modification was applied to the complete hydroxamate inhibitors of the three zinc metallopeptidases (neutral endopeptidase 24-11 (NEP, EC 3.4.24.11), aminopeptidase N (APN, EC 3.4.11.2), and a dipeptidylaminopeptidase (DAP) involved in the in vitro enkephalin degradation by brain tissues. Compounds corresponding to the general formula RN(OH)CO(CH2)(n)CH(CH2Ph)NHCOCH(R')COOH (n=0, 1) were synthesized. In the first series of inhibitors (n=0), the 'retro-inverso' modification induced a large decrease in inhibitory potency for NEP as compared to that of the parent compounds. In contrast, the presence of a methylene group between the hydroxamate and CHα in the second series (n=1) led to derivatives with inhibitory potencies in the nanomolar range, similar to their analogues with a natural amide bond. On the other hand, the retro-inverso modification led to a slight improvement in the inhibition of DAP and APN, in the first series of inhibitors, while the inverse result occurred in the second series. Thus, compounds containing an α-amino acid moiety in P'1 position behave as weak inhibitors of the three enzymes, with IC50 values in the micromolar range, and compounds bearing a β-amino acid moiety in the same position are more specific than the parent compounds for NEP inhibition.