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
• Article Data: 9

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

General Description

Z-PHE-VAL-OH is a synthetic chemical compound that consists of the amino acids phenylalanine (PHE) and valine (VAL) connected by a peptide bond, and a hydroxyl group (OH) at the end. Z-PHE-VAL-OH is often used in peptide synthesis and medical research as a building block for creating peptide-based drugs and pharmaceuticals. Its molecular structure and properties make it suitable for studying the effects of amino acid sequences on peptide structure and function, as well as for developing potential therapeutic agents targeting specific biological pathways. Z-PHE-VAL-OH is an important tool in the study and development of peptide-based drugs, and its precise synthesis and characterization are crucial for its successful application in medical research and drug discovery.

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

• 117999-33-4 Z-ΔPhe-(S)-Val-OH 
• 13518-40-6 L-valine tert-butylester hydrochloride 
• 72-18-4 L-valine 
• 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) 
• 13211-31-9 tert-butyl L-valinate 
• 769922-77-2 (S)-benzyl (1-(1H-benzo[d][1,2,3]triazol-1-yl)-1-oxo-3-phenylpropan-2-yl)carbamate 
• 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 
• 927190-62-3 (-)-N-benzyloxycarbonyl-L-phenylalanine-L-valine thiophenyl ester 
• 29738-92-9 (S)-2-[(S)-2-((S)-2-Benzyloxycarbonylamino-3-phenyl-propionylamino)-3-methyl-butyrylamino]-propionic acid 
• 1449018-07-8 C₂₈H₃₅N₃O₆ 
• 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 
• 69193-11-9 Z-L-Phe-L-Val-NH₂ 
• 55757-64-7 Z-Phe-Val-Pro-OH 

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.

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.

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.