80140-62-1

Basic information

• Product Name: Carbamic acid, [2-[(2,5-dioxo-1-pyrrolidinyl)oxy]-1-[(4-hydroxyphenyl)methyl]-2-oxoethyl] -, phenylmethyl ester, (S)-
• CAS NO: 80140-62-1
• Molecular Formula: C21H20N2O7
• Molecular Weight: 412.399
• Mol File: 80140-62-1.mol
• Article Data: 2

Chemical Properties

• CAS DataBase Reference: Carbamic acid, [2-[(2,5-dioxo-1-pyrrolidinyl)oxy]-1-[(4-hydroxyphenyl)methyl]-2-oxoethyl] -, phenylmethyl ester, (S)-(CAS DataBase Reference)
• NIST Chemistry Reference: Carbamic acid, [2-[(2,5-dioxo-1-pyrrolidinyl)oxy]-1-[(4-hydroxyphenyl)methyl]-2-oxoethyl] -, phenylmethyl ester, (S)-(80140-62-1)
• EPA Substance Registry System: Carbamic acid, [2-[(2,5-dioxo-1-pyrrolidinyl)oxy]-1-[(4-hydroxyphenyl)methyl]-2-oxoethyl] -, phenylmethyl ester, (S)-(80140-62-1)

Safety Data

• Hazardous Substances Data: 80140-62-1(Hazardous Substances Data)

Upstream product

• 75315-63-8 N-(benzyloxycarbonyl)succinimide 
• 60-18-4 L-tyrosine 
• 6066-82-6 1-hydroxy-pyrrolidine-2,5-dione 
• 1164-16-5 Z-L-Tyr-OH 

Downstream Products

• 121888-43-5 Boc-Tyr-Nle-gGly-D-Trp-D-Nle-D-Asp(OBzl)-Z 
• 19898-39-6 N-Carbobenzyloxy-L-tyrosinamide 
• 153077-03-3 (S)-benzyl (1-(4-hydroxyphenyl)-3-oxopropan-2-yl)carbamate 
• 40829-66-1 (S)-2-(benzyloxycarbonylamino)-3-(4-hydroxyphenyl)-1-propanol 
• 1330630-67-5 7-(Nα-benzyloxycarbonyl-L-tyrosyl)amino-4-methylcoumarin 
• 62854-20-0 [(S)-1-Carbamoyl-2-(4-methoxy-phenyl)-ethyl]-carbamic acid benzyl ester 

Relevant articles and documents

Efficient access to enantiopure γ4-amino acids with proteinogenic side-chains and structural investigation of γ4- asn and γ4-ser in hybrid peptide helices

Hybrid peptides composed of α- and β-amino acids have recently emerged as new class of peptide foldamers. Comparatively, γ- and hybrid γ-peptides composed of γ4-amino acids are less studied than their β-counterparts. However, recent investigations reveal that γ4-amino acids have a higher propensity to fold into ordered helical structures. As amino acid side-chain functional groups play a crucial role in the biological context, the objective of this study was to investigate efficient synthesis of γ4-residues with functional proteinogenic side-chains and their structural analysis in hybrid-peptide sequences. Here, the efficient and enantiopure synthesis of various N- and C-terminal free-γ4-residues, starting from the benzyl esters (COOBzl) of N-Cbz-protected (E)-α,β-unsaturated γ-amino acids through multiple hydrogenolysis and double-bond reduction in a single-pot catalytic hydrogenation is reported. The crystal conformations of eight unprotected γ4-amino acids (γ4-Val, γ4-Leu, γ4-Ile, γ4-Thr(OtBu), γ4-Tyr, γ4-Asp(OtBu), γ4- Glu(OtBu), and γ-Aib) reveals that these amino acids adopted a helix favoring gauche conformations along the central Cγi￡ Cβ bond. To study the behavior of γ4- residues with functional side chains in peptide sequences, two short hybrid γ-peptides P1 (Ac-Aib-γ4-Asn-Aib-γ4-Leu- Aib-γ4-Leu-CONH2) and P2 (Ac-Aib- γ4-Ser-Aib-γ4-Val-Aib-γ4-Val- CONH2) were designed, synthesized on solid phase, and their 12-helical conformation in single crystals were studied. Remarkably, the γ4-Asn residue in P1 facilitates the tetrameric helical aggregations through interhelical H bonding between the side-chain amide groups. Furthermore, the hydroxyl side-chain of γ4-Ser in P2 is involved in the interhelical H bonding with the backbone amide group. In addition, the analysis of 87 γ4-residues in peptide single-crystals reveal that the γ4-residues in 12-helices are more ordered as compared with the 10/12- and 12/14-helices. Copyright