17355-18-9

Basic information

• Product Name: H-PHE-TYR-OH
• Synonyms: PHE-TYR;H-PHE-TYR-OH;L-PHENYLALANYL-L-TYROSINE;(S)-2-((S)-2-AMino-3-phenylpropanaMido)-3-(4-hydroxyphenyl)propanoic acid;FY;L-Tyrosine,L-phenylalanyl-;Phe-Tyr-OH≥ 98% (TLC)
• CAS NO: 17355-18-9
• Molecular Formula: C₁₈H₂₀N₂O₄
• Molecular Weight: 328.36
• Mol File: 17355-18-9.mol

Chemical Properties

• Boiling Point: 642.2°Cat760mmHg
• Flash Point: 342.2°C
• Appearance: /
• Density: 1.3g/cm³
• Vapor Pressure: 2.27E-17mmHg at 25°C
• Refractive Index: 1.625
• Storage Temp.: -15°C
• CAS DataBase Reference: H-PHE-TYR-OH(CAS DataBase Reference)
• NIST Chemistry Reference: H-PHE-TYR-OH(17355-18-9)
• EPA Substance Registry System: H-PHE-TYR-OH(17355-18-9)

Safety Data

• Hazardous Substances Data: 17355-18-9(Hazardous Substances Data)

Usage

Chemical Properties

White powder

InChI:InChI=1/C18H20N2O4/c19-15(10-12-4-2-1-3-5-12)17(22)20-16(18(23)24)11-13-6-8-14(21)9-7-13/h1-9,15-16,21H,10-11,19H2,(H,20,22)(H,23,24)/t15-,16-/m0/s1

Upstream product

• 81136-07-4 2-bromo-3-phenylpropionyl chloride 
• 60-18-4 L-tyrosine 
• 35661-40-6 N-Fmoc L-Phe 
• 71989-38-3 Fmoc-Tyr(tBu)-OH 
• 2577-90-4 methyl (2S)-2-amino-3-phenylpropanoate 

Downstream Products

• 1055190-69-6 phenylalanyltyrosine hydrogensquarate 
• 60142-80-5 N-(4-methoxybenzoyl)-phenylalanyltyrosine 
• 63-91-2 L-phenylalanine 

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.

Peptide bond formation by aminolysin-A catalysis: A simple approach to enzymatic synthesis of diverse short oligopeptides and biologically active puromycins

A new S9 family aminopeptidase derived from the actinobacterial thermophile Acidothermus cellulolyticus was cloned and engineered into a transaminopeptidase by site-directed mutagenesis of catalytic Ser491 into Cys. The engineered biocatalyst, designated aminolysin-A, can catalyze the formation of peptide bonds to give linear homo-oligopeptides, hetero-dipeptides, and cyclic dipeptides using cost-effective substrates in a one-pot reaction. Aminolysin-A can recognize several C-terminal-modified amino acids, including the l- and d-forms, as acyl donors as well as free amines, including amino acids and puromycin aminonucleoside, as acyl acceptors. The absence of amino acid esters prevents the formation of peptides; therefore, the reaction mechanism involves aminolysis and not a reverse reaction of hydrolysis. The aminolysin system will be a beneficial tool for the preparation of structurally diverse peptide mimetics by a simple approach.

Compositions and Methods for Binding Lysophosphatidic Acid

Compositions and methods for making and using anti-LPA agents, for example, monoclonal antibodies, are described.