721-90-4

Basic information

• Product Name: H-PHE-GLY-OH
• Synonyms: PHE-GLY;L-PHENYLALANYLGLYCINE;H-PHE-GLY-OH;Phe-Gly hydrate;Phe-glycrystalline;L-Phe-Gly-OH;Phe-Gly-OH;2-[(2-amino-3-phenylpropanoyl)amino]acetic acid
• CAS NO: 721-90-4
• Molecular Formula: C₁₁H₁₄N₂O₃
• Molecular Weight: 222.24
• EINECS: 222-027-9
• Mol File: 721-90-4.mol

Chemical Properties

• Melting Point: ~260 °C (dec.)
• Boiling Point: 512.5°C at 760 mmHg
• Flash Point: 263.7°C
• Appearance: /
• Density: 1.259g/cm³
• Vapor Pressure: 2.51E-11mmHg at 25°C
• Refractive Index: 1.576
• Storage Temp.: -15°C
• PKA: 3.13±0.10(Predicted)
• BRN: 2218143
• CAS DataBase Reference: H-PHE-GLY-OH(CAS DataBase Reference)
• NIST Chemistry Reference: H-PHE-GLY-OH(721-90-4)
• EPA Substance Registry System: H-PHE-GLY-OH(721-90-4)

Safety Data

• Hazard Codes: Xi
• Statements: 36/37/38
• Safety Statements: 22-26-36
• WGK Germany: 3
• F: 3-10
• Hazardous Substances Data: 721-90-4(Hazardous Substances Data)

Usage

Uses

Used in Pharmaceutical Industry:
H-PHE-GLY-OH is used as an active pharmaceutical ingredient for its potential therapeutic effects. The dipeptide structure allows it to interact with specific biological targets, making it a promising candidate for the development of new drugs.
Used in Cosmetics Industry:
In the cosmetics industry, H-PHE-GLY-OH is used as a key ingredient in various skincare and beauty products. Its dipeptide structure contributes to the promotion of skin health and regeneration, making it an essential component in anti-aging and skin repair formulations.
Used in Food and Beverage Industry:
H-PHE-GLY-OH is used as a flavor enhancer and additive in the food and beverage industry. Its dipeptide structure can improve the taste and texture of various products, making it a valuable component in the development of new and improved food items.
Used in Research and Development:
H-PHE-GLY-OH is used as a research tool in the field of biochemistry and molecular biology. Its dipeptide structure allows scientists to study the interactions between different biomolecules, leading to a better understanding of biological processes and the development of new therapeutic strategies.

InChI:InChI=1/C11H14N2O3/c12-9(11(16)13-7-10(14)15)6-8-4-2-1-3-5-8/h1-5,9H,6-7,12H2,(H,13,16)(H,14,15)/t9-/m0/s1

Upstream product

• 99300-27-3 Pht
• 4294-26-2 phenylalanylglycine 
• 63-91-2 L-phenylalanine 
• 30189-51-6 ethyl (N-tert-butoxycarbonyl-L-phenylalanyl)glycinate 
• 2577-90-4 methyl (2S)-2-amino-3-phenylpropanoate 
• 616-34-2 methoxycarbonylmethylamine 
• 5184-17-8 N-benzyloxycarbonyl-L-phenylalanylglycine methyl ester 
• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 25616-33-5 2-((2S)-2-((tert-butoxycarbonyl)amino)-3-phenylpropanamido)acetic acid 
• 1160857-01-1 9-{[2-(O-phenylalanylglycyl)hydroxyethoxy]methyl}guanine trifluoroacetic acid 
• 2075-55-0 S-phenyl (2S)-2-{[(benzyloxy)carbonyl]amino}-3-phenylpropanethioate 
• 13200-85-6 N-formyl-L-phenylalanine 
• 7754-66-7 N-<2-Nitro-benzolsulfenyl>-L-Phe-Gly-OEt 
• 2688-22-4 Nps-L-Phe-OH 

Downstream Products

• 5037-75-2 cyclo(Gly-Phe) 
• 158513-54-3 Ts-Phe-Gly-O-(+)-Men 
• 158419-33-1 N-Ts-L-Phe-Gly-OMe 
• 10125-07-2 3-benzyl-piperazine-2,5-dione 

Relevant articles and documents

A PROCESS FOR PREPARATION OF A PEPTIDE

The present invention relates to a novel process for preparation of peptides having amino acid chain length in the range of 2-40 comprises the steps: i) attaching an end-blocked amino acid with an ionic liquid based solid support in presence of an ionic solvent to obtain an end-terminal blocked amino acid attached ionic liquid; ii) removing end-terminal blocking agent from the end-terminal blocked amino acid attached ionic liquid of step i) followed by work up to obtain an amino acid attached ionic liquid; iii) repeating steps i) through ii) one or more times to obtain a polypeptide attached ionic liquid; and iv) detaching the polypeptide from the polypeptide attached ionic liquid of step iii) to obtain the polypeptide. Said process does not use any auxiliary reagents like dehydrating agent or activating agent. The use of ionic liquids as supports as well as solvents result in the faster kinetics of the process, the separation issues are reduced, and the process has no racemization issues.

Asymmetric Michael addition organocatalyzed by α,β-dipeptides under solvent-free reaction conditions

The application of six novel α,β-dipeptides as chiral organocatalysts in the asymmetric Michael addition reaction between enolizable aldehydes and N-arylmaleimides or nitroolefins is described. With N-arylmaleimides as substrates, the best results were achieved with dipeptide 2 as a catalyst in the presence of aq. NaOH. Whereas dipeptides 4 and 6 in conjunction with 4-dimethylaminopyridine (DMAP) and thiourea as a hydrogen bond donor proved to be highly efficient organocatalytic systems in the enantioselective reaction between isobutyraldehyde and various nitroolefins.

Aggregation propensity of amyloidogenic and elastomeric dipeptides constituents

This study demonstrates the self-assembly of N- and C-terminal protected dipeptides Phe–Gly and Pro–Gly which were derived from amyloidogenic and elastomeric peptide sequences. These constituents afforded nanostructured supramolecular ensembles through va

MgI2-Mediated Chemoselective Cleavage of Protecting Groups: An Alternative to Conventional Deprotection Methodologies

The scope of MgI2 as a valuable tool for quantitative and mild chemoselective cleavage of protecting groups is described here. This novel synthetic approach expands the use of protecting groups, widens the concept of orthogonality in synthetic processes, and offers a facile opportunity to release compounds from solid supports. Amazing MgI2: Protecting groups have had a tremendous positive impact on the art of biomolecule synthesis. In a context in which the use of attractive protecting groups is often limited by harsh deprotection conditions and low chemoselective flexibility, MgI2 offers, by the execution of a very simple protocol, a fresh vision with extensive perspectives.

N -boc deprotection and isolation method for water-soluble zwitterionic compounds

A highly efficient TMSI-mediated deprotection and direct isolation method to obtain zwitterionic compounds from the corresponding N-Boc derivatives has been developed. This method has been demonstrated in the final deprotection/isolation of the β-lactamase inhibitor MK-7655 as a part of its manufacturing process. Further application of this process toward other zwitterionic compounds, such as dipeptides and tripeptides, has been successfully developed. Furthermore, a catalytic version of this transformation has been demonstrated in the presence of BSA or BSTFA.

Microbial enantioselective removal of the N-benzyloxycarbonyl amino protecting group

In order to deprotect N-carbobenzoxy-l-aminoacids (Cbz-AA) and related compounds, a series of microorganisms was selected from soil by enrichment cultures with Cbz-l-Glu as sole nitrogen source. A lyophilized whole-cell preparation of two Arthrobacter sp. strains grown on Cbz-Glu or Cbz-Gly exhibited a high cleavage activity. The conditions of hydrolysis have been optimized and a quantitative enantioselective deprotection of several Cbz-dl-amino acids was obtained, as well as the deprotection of N-carbamoylester derivatives of several synthetic amino compounds. The preparation of Cbz-d-allylglycine and l-allylglycine in high yield and high optical purity is described as an application of this method.

Stereoselective ring contraction of 2,5-diketopiperazines: An innovative approach to the synthesis of promising bioactive 5-membered scaffolds

Ring contraction of 2,5-diketopiperazines by TRAL-alkylation led us to the stereoselective synthesis of original pyrrolidine-2,4-diones, a novel series of promising molecules with moderate anti-proliferative activity on breast cancer cells.

Structure-activity relationships for dipeptide prodrugs of acyclovir: Implications for prodrug design

A series of water-soluble dipeptide ester prodrugs of the antiviral acyclovir (ACV) were evaluated for their chemical stability, cytotoxicity, and antiviral activity against several strains of Herpes Simplex-1 and -2, vaccinia, vesicular stomatitis, cytom

Rates of reduction of N-chlorinated peptides by sulfite: Relevance to incomplete dechlorination of wastewaters

Biologically induced fragmentation of proteins during wastewater treatment produces peptides, which form long-lasting organic chloramines when the water is disinfected with Cl2. To protect aquatic wildlife from residual chlorine, including chloramines, wastewaters are often treated with sulfur dioxide or sulfite salts. This strategy incompletely eliminates residual chlorine species. Here we report that dechlorination rate constants of N- chloropeptides are 1-2 orders of magnitude smaller than those for NH2Cl and some aliphatic organic chloramines. Slow rates explain the prevalence of N- chloropeptides in dechlorinated wastewaters after faster reacting chlorine species have been eliminated. Dechlorination is subject to general acid catalysis. For N-chlorinated leucylalanine, the rate law above pH 6 in phosphate buffer at 25 °C and / ? 0.1 M is as follows: rate = (9.92 ± 0.41 x 103[H2PO4-] + 5.70 ± 0.52 x 108[H3O+] + 5.3 ± 0.2)[SO32-][Cl- Leu-Ala] (concentrations in M, time in s). Rate constants for other peptides appear to be of similar magnitude; variations in the acid-catalyzed terms among different hydrophobic peptides correlate with solvation energies of side chains. The kinetic data suggest that reducing N-chloropeptides in wastewaters by 75% or more will require reaction times generally >0.5 h at environmentally acceptable S(IV) doses and pH values. Biologically induced fragmentation of proteins during wastewater treatment produces peptides, which form long-lasting organic chloramines when the water is disinfected with Cl2. To protect aquatic wildlife from residual chlorine, including chloramines, wastewaters are often treated with sulfur dioxide or sulfite salts. This strategy incompletely eliminates residual chlorine species. Here we report that dechlorination rate constants of N-chloropeptides are 1-2 orders of magnitude smaller than those for NH2Cl and some aliphatic organic chloramines. Slow rates explain the prevalence of N-chloropeptides in dechlorinated wastewaters after faster reacting chlorine species have been eliminated. Dechlorination is subject to general acid catalysis. For N-chlorinated leucylalanine, the rate law above pH 6 in phosphate buffer at 25 °C and I≈0.1 M is as follows: rate = (9.92±0.41×103[H2 PO4- ]+5.70±0.52×108[ H3O+]+5.3±0.2) [SO32-][Cl-Leu-Ala] (concentrations in M, time in s). Rate constants for other peptides appear to be of similar magnitude; variations in the acid-catalyzed terms among different hydrophobic peptides correlate with solvation energies of side chains. The kinetic data suggest that reducing N-chloropeptides in wastewaters by 75% or more will require reaction times generally >0.5 h at environmentally acceptable SIV doses and pH values.

Optimisation of the retroracemisation procedure for α-amino acids using (S)-2-[(N-alkylprolyl)amino]benzophenones, recyclable chiral axiliaries

The retroracemisation procedure developed by Belokon and coworkers has been re-examined using a variety of new (S)-2-[N-alkylprolyl)amino]benzophenone chiral auxiliaries. It has been found that (S)-2-[(N-benzylprolyl)amino] and (S)-2-[(N-1-(naphthalenyl-1-methyl)prolyl)amino] benzophenones ((S)-BPB and (S)-NPB) when used in conjunction with Ni(NO3)2·6H2O and a racemic α-amino acid preferentially form a single diastereoisomer in the presence of a mild base such as sodium methoxide. Decomposition of this complex under acidic conditions leads to the isolation of the (S)-amino acid in good yield, and in 55 to 99% e.e. The retroracemisation abilities of a polymer supported form of the (S)-BPB ligand have also been investigated and preliminary results for this are presented here.