3918-90-9

Basic information

• Product Name: H-PHE-VAL-OH
• Synonyms: L-PHENYLALANYL-L-VALINE;H-PHE-VAL-OH;PHE-VAL;(S)-2-((S)-2-Amino-3-phenylpropanamido)-3-methylbutanoic acid
• CAS NO: 3918-90-9
• Molecular Formula: C₁₄H₂₀N₂O₃
• Molecular Weight: 264.32
• Product Categories: Dipeptides;Dipeptides and Tripeptides;Peptides
• Mol File: 3918-90-9.mol

Chemical Properties

• Boiling Point: 509 °C at 760 mmHg
• Flash Point: 261.7 °C
• Appearance: /
• Density: 1.166 g/cm³
• Vapor Pressure: 3.48E-11mmHg at 25°C
• Refractive Index: 1.549
• Storage Temp.: -15°C
• CAS DataBase Reference: H-PHE-VAL-OH(CAS DataBase Reference)
• NIST Chemistry Reference: H-PHE-VAL-OH(3918-90-9)
• EPA Substance Registry System: H-PHE-VAL-OH(3918-90-9)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 3918-90-9(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Research:
H-PHE-VAL-OH is used as a model compound for studying the behavior and properties of peptides, which aids in the development of new drugs and the understanding of peptide chemistry.
Used in Biochemistry and Molecular Biology:
H-PHE-VAL-OH is utilized as a research tool in the field of biochemistry and molecular biology to explore the interactions and mechanisms of peptides at the molecular level, contributing to the advancement of these scientific disciplines.

InChI:InChI=1/C14H20N2O3/c1-9(2)12(14(18)19)16-13(17)11(15)8-10-6-4-3-5-7-10/h3-7,9,11-12H,8,15H2,1-2H3,(H,16,17)(H,18,19)/t11-,12-/m0/s1

Upstream product

• 68858-20-8 Fmoc-Val-OH 
• 35661-40-6 N-Fmoc L-Phe 
• 63-91-2 L-phenylalanine 
• 108050-48-2 (S)-2-((S)-2-Amino-3-phenyl-propionylamino)-3-methyl-butyric acid benzyl ester 
• 72-18-4 L-valine 
• 583-47-1 L-Phenylalanin-N-carbonsaeureanhydrid 
• 40719-53-7 N-[(S)-2-(2-oxo-4,5-diphenyl-oxazol-3-yl)-3-phenyl-propionyl]-L-valine methyl ester 
• 13123-00-7 (2S)-2-[((2S)-2-{[(benzyloxy)carbonyl]amino}-3-phenylpropanoyl)amino]-3-methylbutanoic acid 
• 37628-66-3 (S)-2-(2-oxo-4,5-diphenyl-oxazol-3-yl)-3-phenyl-propionic acid 

Downstream Products

• 35590-86-4 (3S,6S)-3-(1-methylethyl)-6-(phenylmethyl)piperazine-2,5-dione 

Relevant articles and documents

γ-Valerolactone (GVL): An eco-friendly anchoring solvent for solid-phase peptide synthesis

Due to the hazardous nature of CH2Cl2, regulatory authorities have imposed restrictions to minimize or even stop its use. It has therefore become imperative to identify environmentally benign solvents to replace it. Here we report on a bio derived solvent, γ-valerolactone, for the incorporation of the first amino acid onto p-alkoxybenzyl alcohol resin in solid-phase peptide synthesis. Satisfactory loading values (by a spectrophotometric method) were achieved. Furthermore, racemization and dipeptide formation were also checked and found to be acceptable.

The Steric Hindrance of the Stepwise Reaction of N-Carboxy α-Amino Acid Anhydride with the α-Amino Acid Ester

The mechanisms of the reactions of 4-alkyloxazolidinediones (1) (N-carboxy α-amino acid anhydrides(NCAs)) with α-amino acid benzyl ester p-toluenesulfonates (2) were investigated in acetonitrile containing triethylamine at low and room temperatures.Two types of reactions were observed: (1) the polymerization of NCAs was initiated with a small amount of 2 to produce polypeptides (6), and (2) the dipeptide benzyl esters (4) were produced by the stepwise reaction of NCAs with the esters.Both the polymerization and the dipeptide formation (1+2) seemed to be initiated by the nucleophilic attack of the amino group of the ester on the C-5 carbon of NCAs.The polymerization proceeded when the side chains of the amino acid esters (R2) were more bulky than those of the NCAs (R1).On the contrary, dipeptide esters were produced when the side chains of the NCAs (R1) were more bulky than those of the esters (R2).

Peptides 119. - Peptide Synthesis with N-Carboxy-α-amino Acid Anhydrides

On reaction of N-carboxy-α-amino acid anhydrides (NCA) with equimolar amounts of aminoacids or excess NCA in potassium borate buffer of pH 10.2 (0 deg C) considerable amounts of homooligomers and homopolymers are formed.If an excess of amino acid is used formation of the above mentioned by-products can be suppressed.The extent of homooligomerization and homopolymerization and hydrolysis occurring during the reaction of NCA under the conditions of peptide synthesis is described.