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

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

Uses

Used in Pharmaceutical Applications:
H-GLY-VAL-PHE-OH is used as a therapeutic agent for its potential antioxidant and anti-inflammatory effects, which can contribute to the treatment and management of various diseases and conditions.
Used in Biological Research:
H-GLY-VAL-PHE-OH is used as a research tool to study the mechanisms of various physiological processes, given its role in regulating such processes within the body.
Used in Peptide and Protein Synthesis:
H-GLY-VAL-PHE-OH is used as a building block for the synthesis of larger peptides and proteins, which can be applied in the development of new drugs and therapies.

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 
• 75244-33-6 Z-L-Val-L-Phe-O-t-Bu 
• 16874-17-2 L-phenylalanine tert-butyl ester 
• 15204-61-2 L-Valyl-L-phenylalanin-tert-butylester 

Downstream Products

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

Total Synthesis of PHI

PHI has recently been isolated from porcine duodenum as a new peptide factor with VIP-like activities.Its primary structure corresponds to a linear heptacosapeptide amide characterized by a remarkable sequence homology to the other known members of the gl