13122-91-3

Basic information

• Product Name: N-CARBOBENZOXY-L-PHENYLALANYL-L-PHENYLALANINE
• Synonyms: CBZ-L-PHE-L-PHE;CBZ-L-PHE-PHE;CARBOBENZOXY-L-PHENYLALANYL-L-PHENYLALANINE;N-CBZ-L-PHENYLALANYL-L-PHENYLALANINE;N-CARBOBENZOXY-L-PHENYLALANYL-L-PHENYLALANINE;Z-PHE-PHE-OH;Z-L-PHENYLALANYL-L-PHENYLALANINE;3-phenyl-N-[3-phenyl-N-[(phenylmethoxy)carbonyl]-L-alanyl]-L-alanine
• CAS NO: 13122-91-3
• Molecular Formula: C₂₆H₂₆N₂O₅
• Molecular Weight: 446.5
• EINECS: 236-051-2
• Mol File: 13122-91-3.mol
• Article Data: 25

Chemical Properties

• Melting Point: 159 °C
• Boiling Point: 730.2°Cat760mmHg
• Flash Point: 395.4°C
• Appearance: /
• Density: 1.253g/cm³
• Vapor Pressure: 2.21E-22mmHg at 25°C
• Refractive Index: -10 ° (C=1, MeOH)
• Storage Temp.: -15°C
• Solubility: almost transparency in Methanol
• PKA: 3.53±0.10(Predicted)
• CAS DataBase Reference: N-CARBOBENZOXY-L-PHENYLALANYL-L-PHENYLALANINE(CAS DataBase Reference)
• NIST Chemistry Reference: N-CARBOBENZOXY-L-PHENYLALANYL-L-PHENYLALANINE(13122-91-3)
• EPA Substance Registry System: N-CARBOBENZOXY-L-PHENYLALANYL-L-PHENYLALANINE(13122-91-3)

Safety Data

• Hazardous Substances Data: 13122-91-3(Hazardous Substances Data)

Usage

Chemical Properties

White to off-white powder

Uses

Substrate for cathepsin A.

InChI:InChI=1/C26H26N2O5/c29-24(27-23(25(30)31)17-20-12-6-2-7-13-20)22(16-19-10-4-1-5-11-19)28-26(32)33-18-21-14-8-3-9-15-21/h1-15,22-23H,16-18H2,(H,27,29)(H,28,32)(H,30,31)/t22-,23-/m0/s1

Upstream product

• 71274-26-5 Z-Phe-Phe-OEt(Br) 
• 4892-10-8 N-(benzyloxycarbonyl)-L-phenylalanyl-L-phenylalanine methyl ester 
• 91841-74-6 Boc-Phe-Phe-OPet 
• 2577-40-4 Phe-Phe 
• 501-53-1 benzyl chloroformate 
• 143507-96-4 Z-L-Phe-L-Phe-PNP 
• 150774-34-8 Z-L-Phe-L-Phe p-methoxycarbonylphenyl ester 
• 63-91-2 L-phenylalanine 
• 17543-49-6 (S)-benzyloxycarbonylphenylalanine pentafluorophenyl ester 
• 10466-61-2 (2S)-amino-4-methylpentanamide hydrochloride 
• 252846-40-5 Z-L-Phe-L-Phe-O-carbamoylmethyl 
• 252846-39-2 Z-L-Phe-L-Phe-OCH₂CF₃ 
• 1161-13-3 N-Cbz-L-Phe 
• 2578-84-9 N-benzyloxycarbonyl-L-phenylalanine p-nitrophenyl ester 

Downstream Products

• 91841-74-6 Boc-Phe-Phe-OPet 
• 77738-72-8 (S)-1-[(S)-2-((S)-2-Benzyloxycarbonylamino-3-phenyl-propionylamino)-3-phenyl-propionyl]-pyrrolidine-2-carboxylic acid 4-nitro-phenyl ester 
• 2577-41-5 (S)-benzyl 2-((S)-2-(((benzyloxy)carbonyl)amino)-3-phenylpropanamido)-3-phenylpropanoate 
• 252846-40-5 Z-L-Phe-L-Phe-O-carbamoylmethyl 
• 63-91-2 L-phenylalanine 
• 1161-13-3 N-Cbz-L-Phe 
• 141056-54-4 N-benzyloxycarbonyl-L-phenylalanyl-L-phenylalaninamide 
• 183609-76-9 methyl (R)-1-{(S)-2-[(S)-2-amino-3-phenylpropanamido]-3-phenylpropanoyl}pyrrolidine-2-carboxylate 

Relevant articles and documents

Effects of normal and their branched alcohols with structurally minimal variation on kinetic parameters in thermolysin-catalyzed peptide hydrolysis and synthesis of N-(benzyloxycarbonyl)-L-phenylalanyl-L-phenylalanine and its methyl ester.

When higher alcoholic solvents were added to the reaction medium, and the enhancement of the enzyme activity, followed by its reduction then inactivation, were observed in thermolysin-catalyzed peptide hydrolysis and synthesis. The organic solvent content used was less than the saturating concentration in the buffer (i.e., water-organic one-phase system). The kinetic parameters, Km and kcat, at the alcoholic concentration giving maximal enzyme activity in these reactions changed linearly with increasing logP values of the alcohols and consequently kcat/Km as well. When the branched isomers of alcohols with structurally minimal variation of which logP was equivalent theoretically, were used as annexments, the kinetic parameters were also changed. The results, especially the changes of Km for each organic solvent, suggested that each alcohol should act at the active site of the enzyme in its own effective mode.

Extraordinary Diastereoselectivity Coupled to Altered Structure of Dipeptide Esters

The diastereoselectivity for the hydrolysis of Z-D(L)-Phe-L-Phe p-methoxycarbonylphenyl ester was maximized (ksDL/ksLL=34) at the optimum temperature (30 deg C).This could be attributed to the conformational change in the DL isomer, which was supported by the circular dichroism measurements.

Convenient green preparation of dipeptides using unprotected α-amino acids

Dipeptides and amides were obtained in high yields from N-carbobenzyloxy α-amino acids and 3-phenylpropanoic acid with unprotected α-amino acids via the corresponding mixed carbonic carboxylic anhydrides using ethyl chloroformate and triethylamine by an ecological and convenient method in which the protection of C-terminals is not needed.

Synthesis, bioactivity, docking and molecular dynamics studies of furan-based peptides as 20s proteasome inhibitors

Proteasome inhibitors are promising compounds for a number of therapies, including cardiovascular and eye diseases, diabetes, and cancers. We previously reported a series of furanbased peptidic inhibitors with moderate potencies against the proteasome b5 subunit, hypothesizing that the C-terminal furyl ketone motif could form a covalent bond with the catalytic residue, threonine 1. In this context, we describe further optimizations of the furan-based peptides, and a series of dipeptidic and tripeptidic inhibitors were designed and synthesized, aiming at improved potency and better solubility. Most of the tripeptidic inhibitors demonstrated improved potency and selectivity as b5 subunit inhibitors in both enzymatic and cellular assays, and good antineoplastic activities in various tumor cell lines were also observed. However, no inhibitory effects were observed for the dipeptidic compounds, which led us to presume that a noncovalent binding mode is adopted. Docking studies and molecular dynamics simulations were carried out to verify this presumption, with results showing that the distance between the furyl ketone motif and Thr1 is slightly too long to form covalent bond.