82985-55-5

Basic information

• Product Name: H-GLY-VAL-PHE-OH
• Synonyms: H-GLY-VAL-PHE-OH
• CAS NO: 82985-55-5
• Molecular Formula: C₁₆H₂₃N₃O₄
• Molecular Weight: 321.37
• Mol File: 82985-55-5.mol
• Article Data: 2

Chemical Properties

• Appearance: /
• Storage Temp.: -15°C
• CAS DataBase Reference: H-GLY-VAL-PHE-OH(CAS DataBase Reference)
• NIST Chemistry Reference: H-GLY-VAL-PHE-OH(82985-55-5)
• EPA Substance Registry System: H-GLY-VAL-PHE-OH(82985-55-5)

Safety Data

• Hazardous Substances Data: 82985-55-5(Hazardous Substances Data)

Usage

General Description

H-GLY-VAL-PHE-OH, also known as glycyl-valyl-phenylalanine, is a peptide composed of three amino acids linked together. The chemical structure consists of a glycine (Gly), valine (Val), and phenylalanine (Phe) amino acid residues linked by peptide bonds, with an N-terminal hydrogen (H) and a C-terminal hydroxyl (OH) group. This peptide is commonly used in biological research and pharmaceutical applications for its potential therapeutic properties, such as antioxidant and anti-inflammatory effects, as well as its ability to regulate various physiological processes in the body. It is also used as a building block for the synthesis of larger peptides and proteins.

Upstream product

• 82985-54-4 Boc-Gly-Val-Phe-OBu-t 
• 3918-92-1 L-valyl L-phenylalanine 
• 3496-11-5 2,5-dioxopyrrolidin-1-yl (2S)-2-(((benzyloxy)carbonyl)amino)-3-methylbutanoate 
• 16874-17-2 L-phenylalanine tert-butyl ester 
• 15204-61-2 L-Valyl-L-phenylalanin-tert-butylester 
• 75244-33-6 Z-L-Val-L-Phe-O-t-Bu 

Downstream Products

• 82985-56-6 Z-Asp(OBu-t)-Gly-Val-Phe-OH 
• 82985-57-7 H-Asp(OBu-t)-Gly-Val-Phe-OH 
• 82985-59-9 H-Ala-Asp(OBu-t)-Gly-Val-Phe-OH 
• 82985-58-8 Z-Ala-Asp(OBu-t)-Gly-Val-Phe-OH 

Relevant articles and documents

Inhibitors of tripeptidyl peptidase II. 2. Generation of the first novel lead inhibitor of cholecystokinin-8-inactivating peptidase: A strategy for the design of peptidase inhibitors

The cholecystokinin-8 (CCK-8)-inactivating peptidase is a serine peptidase which has been shown to be a membrane-bound isoform of tripeptidyl peptidase II (EC 3.4.14.10). It cleaves the neurotransmitter CCK-8 sulfate at the Met-Gly bond to give Asp-Tyr(SO3H)-Met-OH + Gly-Trp-Met-Asp-Phe-NH2. In seeking a reversible inhibitor of this peptidase, the enzymatic binding subsites were characterized using a fluorimetric assay based on the hydrolysis of the artificial substrate Ala-Ala-Phe-amidomethylcoumarin. A series of di- and tripeptides having various alkyl or aryl side chains was studied to determine the accessible volume for binding and to probe the potential for hydrophobic interactions. From this initial study the tripeptides Ile-Pro-Ile-OH (K(i) = 1 μM) and Ala-Pro-Ala-OH (K(i) = 3 μM) and dipeptide amide Val-Nvl-NHBu (K(i) = 3 μM) emerged as leads. Comparison of these structures led to the synthesis of Val-Pro-NHBu (K(i) = 0.57 μM) which served for later optimization in the design of butabindide, a potent reversible competitive and selective inhibitor of the CCK-8-inactivating peptidase. The strategy for this work is explicitly described since it illustrates a possible general approach for peptidase inhibitor design.