6234-26-0

Basic information

• Product Name: H-GLY-GLY-PHE-OH
• Synonyms: GLY-GLY-PHE;GLYCYL-GLYCYL-L-PHENYLALANINE;H-GLY-GLY-PHE-OH;(S)-2-[(N-Glycylglycyl)amino]-3-phenylpropionic acid;Gly-Gly-L-Phe-OH;Gly-Gly-Phe-OH;(S)-2-(2-(2-AMinoacetaMido)acetaMido)-3-phenylpropanoic acid;Enkephalin (2-4)
• CAS NO: 6234-26-0
• Molecular Formula: C₁₃H₁₇N₃O₄
• Molecular Weight: 279.29
• Mol File: 6234-26-0.mol

Chemical Properties

• Melting Point: 228-230 °C (decomp)
• Boiling Point: 417.6°C at 760 mmHg
• Flash Point: 206.4°C
• Appearance: /
• Density: 1.13g/cm³
• Vapor Pressure: 3.49E-07mmHg at 25°C
• Refractive Index: 1.548
• Storage Temp.: -15°C
• PKA: 3.47±0.10(Predicted)
• CAS DataBase Reference: H-GLY-GLY-PHE-OH(CAS DataBase Reference)
• NIST Chemistry Reference: H-GLY-GLY-PHE-OH(6234-26-0)
• EPA Substance Registry System: H-GLY-GLY-PHE-OH(6234-26-0)

Safety Data

• Hazardous Substances Data: 6234-26-0(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
H-GLY-GLY-PHE-OH is used as a pharmaceutical candidate for various applications due to its unique structure and properties.
Used in Cosmetic Industry:
H-GLY-GLY-PHE-OH is used as an ingredient in cosmetic products for its potential benefits to the skin, such as promoting collagen production and improving skin elasticity.
Used in Research and Development:
H-GLY-GLY-PHE-OH is used as a research compound for studying the properties and potential applications of peptides in various fields, including medicine, biotechnology, and materials science.

InChI:InChI=1/C14H16FNO/c15-12-8-5-11(6-9-12)7-10-14(17)16-13-3-1-2-4-13/h5-10,13H,1-4H2,(H,16,17)/b10-7+

Upstream product

• 75720-14-8 1-O-(glycylglycyl-L-phenylalanyl)-β-D-glucopyranose trifluoroacetate 
• 75719-93-6 2,3,4,6-tetra-O-benzyl-1-O-(N-benzyloxycarbonylglycylglycyl-D-phenylalanyl)-β-D-glucopyranose 
• 13171-93-2 N-benzyloxycarbonyl-L-glycyl-L-glycyl-L-phenylalanine 
• 29022-11-5 N-(fluoren-9-ylmethoxycarbonyl)glycine 
• 58822-25-6 Leu-enkephalin 

Downstream Products

• 89178-06-3 ({[((S)-1-Methoxycarbonyl-2-phenyl-ethylcarbamoyl)-methyl]-carbamoyl}-methyl)-trimethyl-ammonium 
• 24853-77-8 N-benzoylglycylglycyl-L-phenylalanine 
• 63-91-2 L-phenylalanine 
• 56-40-6 glycine 
• 68800-26-0 N-tert-butoxycarbonylglycylglycylphenylalanylmethionine 
• 83380-11-4 glycylglycylphenylalanylmethioninamide hydrochloride 
• 83380-12-5 (-)-(2R,6R,11R)-<(1,2,3,4,5,6-hexahydro-8-hydroxy-3,6,11-trimethyl-2,6-methano-3-benzazocin-4-yl)carbonyl>glycylglycylphenylalanylmethioninamide 
• 83380-12-5 (+)-(2S,6S,11S)-<(1,2,3,4,5,6-hexahydro-8-hydroxy-3,6,11-trimethyl-2,6-methano-3-benzazocin-4-yl)carbonyl>glycylglycylphenylalanylmethioninamide 
• 19137-07-6 bis(2,2':6',2''-terpyridine)cobalt(III) 
• 859234-85-8 (C₁₅H₁₁N₃)Co[HN(CO)2NCH(CH₂C₆H₅)COO] 

Relevant articles and documents

Rapid and controllable hydrogen/deuterium exchange on aromatic rings of α-amino acids and peptides

Novel hydrogen/deuterium exchange for aromatic α-amino acids and their corresponding peptides were performed through the use of deuterated trifluoromethanesulfonic acid (TfOD). Detailed analysis of the exchange revealed that equal hydrogen/deuterium excha

A genetically encodable ligand for transfer hydrogenation

Simple tripeptides are shown here to be versatile ligands for iridium-catalyzed transfer hydrogenations affording large acceleration effects. A water-soluble iridium complex with Gly-Gly-Phe, for example, catalyzes the reduction of diverse ketones, aldehydes, and imines by formate with turnover frequencies rivaling or outperforming those of established ligand systems. Regioselective reduction of coenzyme NAD+ to NADH illustrates the potential utility of this system for biotechnological applications. Because peptides are genetically encodable, they represent an attractive class of foldamer ligands for creating artificial metalloenzymes.

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.

Pharmaceutical preparations having diuretic activity

Pharmaceutical preparations having diuretic activity and comprising a peptide of the formula STR1 wherein (a) R1 and R2 are hydrogen and R3 is --OH, or STR2 or Y, or wherein (b) R1 is hydrogen, R2 is CH2 OH or STR3 and R3 is --OH or Y, or wherein (c) R1 is --CH2 OH and R2 is hydrogen or STR4 and R3 is --OH or Y, or wherein (d) R1 is STR5 R2 is hydrogen or --CH2 OH and R3 is --OH, --NHCH2 COOH, or Y, and wherein X is hydrogen, methyl, prolyl, or an N-protective group, and Y is --NH2, --OR4, wherein R4 is linear or branched alkyl or cyclolalkyl having from 1 to 8 carbon atoms, benzyl, phenyl, or STR6

SYNTHESIS, PROPERTIES, AND REACTIONS OF α- AND β-D-GLUCOPYRANOSYL ESTERS OF SOME TRIPEPTIDES

The 2,3,4,6-tetra-O-benzyl-1-O-(N-benzyloxycarbonyltripeptidyl)-D-glucopyranoses 1, 8, and 13 were synthesised from 2,3,4,6-tetra-O-benzyl-α-D-glucopyranose and the active esters of the appropriate N-protected tripeptides (Gly-Gly-Gly-, L-Phe-Gly-Gly-, and Gly-Gly-L-Phe-) in the presence of imidazole; the anomeric mixtures were resolved and the α and β anomers characterised.The β anomer of 13, containing the L and D enantiomers (ratio ca. 3:1) of Gly-Gly-Phe- as the aglycon, could be resolved by column chromatography into the pure isomeric forms.Catalytic hydrogenolysis of the β anomers, in the presence and absence of a strong acid, yielded the free 1-esters 2β, 9β, and 14β, which were characterised as the mono-oxalate or trifluoroacetate salts and as free bases.Similarly, the α anomers afforded 2α, 9α, and 14α, whereas omission of the strong acid led to accompanying 1 --> 2 acyl migration, to give the 2-O-acyl derivatives.All of the compounds prepared were converted into the N-acetyl and/or peracetylated derivatives.The 1-esters 2β and 9β, both in the charged and uncharged form, and the trifluoroacetate salt of 14β, are susceptible to cleavage by β-D-glucosidase; the enzyme had no effect on the uncharged form of 14β.This difference between 14β and its salt is discussed in conformational terms.