13122-99-1

Basic information

• Product Name: Z-PHE-GLY-OH
• Synonyms: N-CBZ-PHE-GLY;N-CARBOBENZOXY-L-PHENYLALANYLGLYCINE;N-BENZYLOXYCARBONYL-L-PHENYLALANYLGLYCINE;Z-PHE-GLY;Z-PHE-GLY-OH;Z-L-PHENYLALANYL-GLYCINE;Z-L-PHENYLALANYL-L-GLYCINE;CBZ-L-PHE GLY
• CAS NO: 13122-99-1
• Molecular Formula: C19H20N2O5
• Molecular Weight: 356.37
• EINECS: 236-052-8
• Product Categories: Dipeptides;Dipeptides and Tripeptides;Peptides
• Mol File: 13122-99-1.mol
• Article Data: 17

Chemical Properties

• Boiling Point: 669.9°Cat760mmHg
• Flash Point: 358.9°C
• Appearance: /
• Density: 1.278g/cm³
• Vapor Pressure: 7.37E-19mmHg at 25°C
• Refractive Index: 1.589
• Storage Temp.: −20°C
• CAS DataBase Reference: Z-PHE-GLY-OH(CAS DataBase Reference)
• NIST Chemistry Reference: Z-PHE-GLY-OH(13122-99-1)
• EPA Substance Registry System: Z-PHE-GLY-OH(13122-99-1)

Safety Data

• WGK Germany: 3
• Hazardous Substances Data: 13122-99-1(Hazardous Substances Data)

Usage

Chemical Properties

White powder

Uses

Substrate for carboxypeptidase Y from baker's yeast.

InChI:InChI=1/C19H20N2O5/c22-17(23)12-20-18(24)16(11-14-7-3-1-4-8-14)21-19(25)26-13-15-9-5-2-6-10-15/h1-10,16H,11-13H2,(H,20,24)(H,21,25)(H,22,23)/t16-/m0/s1

Upstream product

• 2778-34-9 ethyl [(2S)-2-(benzyloxycarbonylamino)-3-phenylpropanoylamino]acetate 
• 4864-80-6 benzyl (S)-(1-((2-hydroxyethyl)amino)-1-oxo-3-phenylpropan-2-yl)carbamate 
• 2578-84-9 N-benzyloxycarbonyl-L-phenylalanine p-nitrophenyl ester 
• 56-40-6 glycine 
• 78605-45-5 [(S)-1-Benzyl-2-oxo-2-(2-oxo-oxazol-3-yl)-ethyl]-carbamic acid benzyl ester 
• 721-90-4 (S)-PheGly 
• 64-17-5 ethanol 
• 62076-41-9 Cbz-Phe-Gly-Ser-OMe 
• 769922-77-2 (S)-benzyl (1-(1H-benzo[d][1,2,3]triazol-1-yl)-1-oxo-3-phenylpropan-2-yl)carbamate 
• 1059596-58-5 N-Cbz-L-phenylalanine p-tolylthiol ester 
• 6372-14-1 N-((benzyloxy)carbonyl)-L-phenylalaninol 
• 59830-60-3 benzyl (1S)-(1-formyl-2-phenylethyl)carbamate 
• 3182-95-4 L-Phenylalaninol 
• 501-53-1 benzyl chloroformate 

Downstream Products

• 63069-10-3 N-[N-(N-benzyloxycarbonyl-L-phenylalanyl)-glycyl]-L-tyrosine amide 
• 53412-29-6 Z-Phe-Gly-NH-NH-Boc 
• 96452-62-9 N-(Benzyloxycarbonyl)-L-Phe-Gly-2-pyridylester 
• 59180-32-4 ((S)-1-{[({4-Chloro-2-[(2-chloro-phenyl)-hydroxy-methyl]-phenyl}-methyl-carbamoyl)-methyl]-carbamoyl}-2-phenyl-ethyl)-carbamic acid benzyl ester 
• 66963-75-5 C₅₈H₆₈N₆O₁₅ 
• 37700-64-4 (5S)-5-benzyl-3,6,9-trioxo-1-phenyl-2-oxa-4,7,10-triazadodecan-12-oic acid 
• 1286678-64-5 (S)-benzyl (1-((2-(1H-benzo[d][1,2,3]triazol-1-yl)-2-oxoethyl)amino)-1-oxo-3-phenyl-propan-2-yl)carbamate 
• 62107-97-5 Phenylalanyl-glycinanhydrid 
• 74075-25-5 Bz-Phe-Gly-Pro 
• 74075-24-4 Phe-Gly-Pro 
• 96452-63-0 Z-L-Phe-Gly-L-Phe-OtBu 
• 87053-84-7 Z-L-Phe-Gly-L-Phe-OMe 

Relevant articles and documents

Chemoselective Intramolecular Formal Insertion Reaction of Rh–Nitrenes into an Amide Bond Over C?H Insertion

The past few decades have witnessed extensive efforts to disclose the unique reactivity of metal–nitrenes, because they could be a powerful synthetic tool for introducing the amine functionality into unactivated chemical bonds. The reactivity of metal–nitrenes, however, is currently mainly confined to aziridination (an insertion into a C=C bond) and C?H amination (an insertion into a C?H bond). Nitrene insertion into an amide C?N bond, however, has not been reported so far. In this work we have developed a rhodium-catalyzed one-nitrogen insertion into amide C?N and sulfonamide S?N bonds. Experimental and theoretical analyses based on density functional theory indicate that the formal amide insertion proceeds via a rhodium-coordinated ammonium ylide formed between the nitrene and the amide nitrogen, followed by acyl group transfer concomitant with C?N bond cleavage. Mechanistic studies have allowed rationalization of the origin of the chemoselectivity observed between the C?H and amide insertion reactions. The methodology presented herein is the first example of an insertion of nitrene into amide bonds and provides facile access to unique diazacyclic systems with an N?N bond linkage.

Scandium(III) triflate-promoted serine/threonine-selective peptide bond cleavage

The site-selective cleavage of peptide bonds is an important chemical modification that is useful not only for the structural determination of peptides, but also as an artificial modulator of peptide/protein function and properties. Here we report site-selective hydrolysis of peptide bonds at the Ser and Thr positions with a high conversion yield. This chemical cleavage relies on Sc(iii)-promoted N,O-acyl rearrangement and subsequent hydrolysis. The method is applicable to a broad scope of polypeptides with various functional groups, including a post-translationally modified peptide that is unsuitable for enzymatic hydrolysis. The system was further extended to site-selective cleavage of a native protein, Aβ1-42, which is closely related to the onset of Alzheimer's disease.

Discovery of Fluoromethylketone-Based Peptidomimetics as Covalent ATG4B (Autophagin-1) Inhibitors

ATG4B or autophagin-1 is a cysteine protease that cleaves ATG8 family proteins. ATG4B plays essential roles in the autophagosome formation and the autophagy pathway. Herein we disclose the design and structural modifications of a series of fluoromethylketone (FMK)-based peptidomimetics as highly potent ATG4B inhibitors. Their structure-activity relationship (SAR) and protease selectivity are also discussed.