13123-00-7

Basic information

• Product Name: Z-PHE-VAL-OH
• Synonyms: Z-PHE-VAL-OH;Z-L-PHENYLALANYL-L-VALINE;N-CBZ-L-PHENYLALANYL-L-VALINE;N-[N-[(benzoyloxy)carbonyl]-L-phenylalanyl]-L-valine;N-benzyloxycarbonylphenylalanyl-valine;Cbz-L-Phe-L-Val-OH;N-[(S)-2-[[(Phenylmethoxy)carbonyl]amino]-3-phenylpropionyl]-L-valine;Z-L-Phe-L-Val-OH
• CAS NO: 13123-00-7
• Molecular Formula: C₂₂H₂₆N₂O₅
• Molecular Weight: 398.45
• EINECS: 236-053-3
• Mol File: 13123-00-7.mol

Chemical Properties

• Melting Point: 145-146 °C
• Boiling Point: 668.9°C at 760 mmHg
• Flash Point: 358.3°C
• Appearance: /
• Density: 1.211g/cm³
• Vapor Pressure: 8.36E-19mmHg at 25°C
• Refractive Index: 1.569
• Storage Temp.: -15°C
• PKA: 3.44±0.10(Predicted)
• CAS DataBase Reference: Z-PHE-VAL-OH(CAS DataBase Reference)
• NIST Chemistry Reference: Z-PHE-VAL-OH(13123-00-7)
• EPA Substance Registry System: Z-PHE-VAL-OH(13123-00-7)

Safety Data

• Hazardous Substances Data: 13123-00-7(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
Z-PHE-VAL-OH is used as a building block in the synthesis of peptide-based drugs for its ability to contribute to the development of new pharmaceuticals with specific therapeutic properties.
Used in Medical Research:
Z-PHE-VAL-OH is used as a research tool for studying the effects of amino acid sequences on peptide structure and function, aiding in the understanding of peptide behavior and the discovery of potential therapeutic agents.
Used in Drug Discovery:
Z-PHE-VAL-OH is utilized in the development of potential therapeutic agents targeting specific biological pathways, highlighting its importance in the advancement of medical treatments and interventions.

InChI:InChI=1/C22H26N2O5/c1-15(2)19(21(26)27)24-20(25)18(13-16-9-5-3-6-10-16)23-22(28)29-14-17-11-7-4-8-12-17/h3-12,15,18-19H,13-14H2,1-2H3,(H,23,28)(H,24,25)(H,26,27)

Upstream product

• 72-18-4 L-valine 
• 769922-77-2 (S)-benzyl (1-(1H-benzo[d][1,2,3]triazol-1-yl)-1-oxo-3-phenylpropan-2-yl)carbamate 
• 13211-31-9 tert-butyl L-valinate 
• 13518-40-6 L-valine tert-butylester hydrochloride 
• 117999-33-4 Z-ΔPhe-(S)-Val-OH 
• 1161-13-3 N-Cbz-L-Phe 
• 6306-52-1 L-valine methylester hydrochloride 
• 4818-08-0 N-Z-L-phenylalanyl-L-valine methylester 
• 109453-49-8 (C₈H₇O₂)(NHCHCOO)(CH₂C₆H₅)(CO₂C₂H₅) 
• 2688-15-5 3-Methyl-1-phenyl-5-(Z-DL-phenylalanyloxy)-pyrazol 
• 14470-31-6 (S)-tert-butyl 2-((S)-2-(((benzyloxy)carbonyl)amino)-3-phenylpropanamido)-3-methylbutanoate 
• 3397-32-8 N-(benzyloxycarbonyl)-phenylalanine-N-hydroxysuccinimide ester 

Downstream Products

• 164861-48-7 Z-L-Phe-L-Val-L-Pro-NH₂ 
• 29738-92-9 (S)-2-[(S)-2-((S)-2-Benzyloxycarbonylamino-3-phenyl-propionylamino)-3-methyl-butyrylamino]-propionic acid 
• 69193-11-9 Z-L-Phe-L-Val-NH₂ 
• 128228-51-3 [(S)-1-((S)-4-Isopropyl-5-oxo-4,5-dihydro-oxazol-2-yl)-2-phenyl-ethyl]-carbamic acid benzyl ester 
• 82213-51-2 Z-Phe-Val-Pro-OBu^t 
• 82213-52-3 Z-Phe-D-Val-Pro-OBu^t 
• 3918-90-9 L-phenylalanyl-L-valine 
• 1449018-07-8 C₂₈H₃₅N₃O₆ 

Relevant articles and documents

Epimerization-Free C-Term Activation of Peptide Fragments by Ball Milling

Peptides were produced in high yields and, if any, very low epimerization, by mechanochemical coupling of peptide fragments containing highly epimerization-prone and/or highly hindered amino acids at C-term. Ball milling was clearly identified as the key element enabling one to obtain such results.

A catalytic one-step synthesis of peptide thioacids: the synthesis of leuprorelin via iterative peptide-fragment coupling reactions

A catalytic one-step synthesis of peptide thioacids was developed. The oxygen-sulfur atom exchange reaction converted the carboxy group at the C-terminus of the peptides into a thiocarboxy group with suppressed epimerization. This method was successfully applied to the synthesis of the peptide drug leuprorelin via an iterative fragment-coupling protocol.

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.

Design and synthesis of novel hydroxypyridinone derivatives as potential tyrosinase inhibitors

Two groups of novel hydroxypyridinone derivatives 6(a-e) and 12(a-c), were designed as potential tyrosinase inhibitors, and synthesized using kojic acid as a starting material. The tyrosinase inhibitory activity of these two groups was demonstrated to be potent, especially compounds 6e and 12a, whose IC50 values for monophenolase activity were 1.95 μM and 2.79 μM, respectively. Both of these values are lower than that of kojic acid (IC50 = 12.50 μM). Compounds 6e and 12a were investigated for the inhibitory effect on diphenolase activity. The results showed that the inhibitory mechanism of these two compounds was reversible and that the inhibitory type was a competitive-uncompetitive mixed-type. The values of IC50 of 6e and 12a on the diphenolase activity of tyrosinase were determined to be 8.97 μM and 26.20 μM, respectively. The inhibitory constants (KI and KIS) of 6e were determined as 17.17 μM and 22.09 μM, respectively; and the KI and KIS values of 12a were 34.41 μM and 79.02 μM, respectively. Compound 6e showed a greater ability to reduce copper and a stronger copper chelating ability than kojic acid.

Convenient peptide synthesis without protection of C-Terminals

Condensation of carboxylic acids 1 and 5 with unprotected α-amino acids 2 via activation by ethyl chloroformate and triethylamine proceeded effectively to afford the corresponding amides in 5099% yields. Tripeptide 7c was obtained in 42% yield from the dipeptide 6c in a similar manner.

Highly diastereoselective peptide chain extensions of unprotected amino acids with N-(Z-α-aminoacyl)benzotriazoles

Coupling an unprotected amino acid or dipeptide in partially aqueous solution with a readily available N-(Z-α-amino-acyl)benzotriazole or N-(Z-α-aminopetidoyl)benzotriazole affords N-terminal-protected di-, tri-, and tetrapeptides in yields of 85-98% (average 95% for 2a-i, 93% for 4a-f and 4a′, 86% for 5a-b) with minimal epimerization.

In the search for new anticancer drugs. XXIV: Synthesis and anticancer activity of amino acids and dipeptides containing the 2-chloroethyl- and [N'- (2-chloroethyl)-N'-nitroso]-aminocarbonyl groups

A series of L,L-(42, 44, 46, and 60) and D,D-(43, 45, 47, and 61) dipeptide derivatives composed of phenylglycine, phenylalanine, homophenylalanine, and valine and containing a 2-chloroethylamino group at the C-terminus and an N'-(2-chloroethyl)-N'-nitrosoaminocarbonyl group at the N-terminus of the dipeptides were prepared. The dipeptide derivatives (42- 47, 60, and 61) were first evaluated in vivo for their anticancer activities against the murine lymphocytic leukemia P388. Compounds 42, 44, 46, and 60 possessed activities ranging from 46 to 111 percent increase in life span (%ILS), whereas 43 was marginal (%ILS = 31) and 45, 47, and 61 were inactive. In general, the L,L-series exhibited low to good activity (%ILS = 46-111), whereas the corresponding D,D-series, except for 43 (%ILS = 31), was devoid of activity. The analogously structured monoamino acid derivatives of L- alanine (74), L-phenylalanine (75), and L-aspartic acid (76) exhibited higher activity against P388 than the dipeptide derivatives (i.e., 481, 297, and 481 %ILS, respectively). The more active representatives of dipeptides (i.e., 42, 44, and 60) and the amino acids derivatives 74-76 were then tested in vivo against the murine lymphoid leukemia L1210. Compounds 42, 44, and 60 exhibited either low or marginal activity (i.e., the %ILS values were 46, 31, and 26, respectively). Compounds 74, 75, and 76 possessed low to moderate activity, as evidenced by the %ILS values of 56, 48, and 64, respectively. The %ILS parameters obtained against the P388 and L1210 tumor lines were correlated with the corresponding lipophilicities, and there is a trend towards higher activity with concomitant decrease in hydrophobicity.

Efficient 1,4-Asymetric Induction Utilizing Electrostatic Interaction between Ligand and Substrate in the Asymmetric Hydrogenation of Didehydrodipeptides

Electrostatic interaction between the amino group of the achiral 3-dimethylaminopropylidenebismethylenebis(diphenylphosphine) (1) and the carboxy group of the substrate enable an effective 1,4-asymmetric induction in the RhI-catalysed hydrogenation of didehydrodipeptides, to give (S,S)-or (R,R)-products selectively.The selectivity reached up to 94percent diastereoisomeric excess with acetyl didehydrodipeptides and 92percent with benzyloxycarbonyl substrates.