13122-99-1

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

• 2075-55-0 S-phenyl (2S)-2-{[(benzyloxy)carbonyl]amino}-3-phenylpropanethioate 
• 56-40-6 glycine 
• 1161-13-3 N-Cbz-L-Phe 
• 2778-34-9 ethyl [(2S)-2-(benzyloxycarbonylamino)-3-phenylpropanoylamino]acetate 
• 5184-17-8 N-benzyloxycarbonyl-L-phenylalanylglycine methyl ester 
• 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 
• 78605-45-5 [(S)-1-Benzyl-2-oxo-2-(2-oxo-oxazol-3-yl)-ethyl]-carbamic acid benzyl ester 
• 721-90-4 (S)-PheGly 
• 3086-21-3 Z-Phe-O-Pcp 
• 3182-95-4 L-Phenylalaninol 
• 59830-60-3 benzyl (1S)-(1-formyl-2-phenylethyl)carbamate 
• 6372-14-1 N-((benzyloxy)carbonyl)-L-phenylalaninol 
• 1059596-58-5 N-Cbz-L-phenylalanine p-tolylthiol ester 

Downstream Products

• 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 
• 16336-36-0 N-Carbobenzoxy-phenylalanin-glycin-p-nitrophenylester 
• 57294-43-6 Cbz-Phe-Gly-OBn 
• 175918-21-5 (S)-2-({(R)-1-[2-((S)-2-Benzyloxycarbonylamino-3-phenyl-propionylamino)-acetylamino]-2-phenyl-ethyl}-methoxy-phosphinoyloxy)-3-phenyl-propionic acid 3-pyridin-4-yl-propyl ester 
• 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 
• 63069-10-3 N-[N-(N-benzyloxycarbonyl-L-phenylalanyl)-glycyl]-L-tyrosine amide 

Relevant academic research and scientific papers

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.

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.

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.

Synthesis and evaluation of novel benzimidazole conjugates incorporating amino acids and dipeptide moieties

Background: Amino acids, short peptide sequences and benzimidazole derivatives play an increasingly important role as therapeutics in areas including antibacterial, antifungal, antiviral, antiinflammatory, antiparasitic, antibiofilm, antidiabetic, and anticancer. Methods: Some novel amino acids and glycine-glycine dipeptide benzimidazole conjugates were synthesized by facile acylation reactions through DCC mediated reactions and their structures were identified by 1H-NMR, 13C-NMR and FT-IR spectroscopic techniques and elemental analysis. In vitro antimicrobial activities of some compounds against Gram positive (Staphylococcus aureus and Enterobacter faceium NJ-1) and Gram negative bacteria (Escherichia coli and Pseudomonas aeruginosa), and yeasts (Candida albicans and Candida tropicalis) were determined by MIC method. Their antioxidant activities were also detected by DPPH method. Results: Sixteen novel benzimidazole conjugates incorporating glycine, alanine, phenylalanine, cysteine and glycine-glycine dipeptide were synthesized and their structures were identified by spectroscopic techniques and elemental analysis. All of the compounds tested showed in vitro antimicrobial and antioxidant activities. Conclusion: Sixteen novel benzimidazole amino acid/dipeptide conjugates were synthesized using DCC mediated one step reaction in moderate yield and high purity, under mild reaction conditions, with full retention of the original chirality. Amino acid or dipeptide substitutions at position 1 of the benzimidazoles were synthesized first time in this work. The results have indicated that the newly synthesized compounds possess low to moderate antimicrobial and antioxidant activities.

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.

Synthesis, molecular docking and anticancer studies of peptides and iso-peptides

Chiral peptides and iso-peptides were synthesized in excellent yield by using benzotriazole mediated solution phase synthesis. Benzotriazole acted both as activating and leaving group, eliminating frequent use of protection and subsequent deprotection. The procedure was based on the hypothesis that epimerization should be suppressed in solution due to a faster coupling rate than SPPS. All the synthesized peptides complied with Lipinski's Ro5 except for the rotatable bonds. Inhibition of cell proliferation of cancer cell lines is one of the most commonly used methods to study the effectiveness of any anticancer agents. Synthesized peptides and iso-peptides were tested against three cancer cell lines (MCF-7, MDA-MB 231) to determine their anti-proliferative potential. NFkB was also determined. Molecular docking studies were also carried out to complement the experimental results.

HMDO-promoted peptide and protein synthesis in ionic liquids

Hexamethyldisiloxane (HMDO) has been developed to efficiently promote the metal-free direct coupling of an amino function of one cysteine-free peptide or protein and a C-terminal thioester of the second peptide in ionic liquids. The amide-coupling reaction proceeds smoothly under mild conditions to afford the corresponding products in good to excellent yields (63-94%). Peptide couplings were also achieved using in-situ-generated thioesters by the thioesterification of oxo esters.

Influence of solvent viscosity on the rate of hydrolysis of dipeptides by carboxypeptidase Y

The influence of solvent viscosity on the rate of enzymatic hydrolysis of a series of dipeptides (Z-Phe-Gly, Z-Phe-Sar, Z-Phe-Ala, Z-Phe-NMeAla, Z-Phe-Aib and Z-Phe-Pro) by carboxypeptidase Y was investigated. The effect of solvent viscosity on the enzymatic hydrolysis revealed that whereas all Kcat values decreased with viscosity, those of the N-alkyl peptides decreased more than those of the N-H peptides. The kinetic behaviour implies the involvement of conformational changes of the enzyme in terms of the 'induced-fit' process. Copyright

Relationship between the hydrophobicity of dipeptides and the Michaelis-Menten constant Km of their hydrolysis by carboxypeptidase-Y and carboxypeptidase-A

The enzymatic hydrolysis of dipeptides by carboxypeptidase-Y and carboxypeptidase-A was investigated. In the enzymatic hydrolysis of the dipeptides, a good linear relationship (r = 0.997 and 0.999) was found between the Michaelis-Menten constant (Km) and the hydrophobicity of the substrates evaluated from relative elution volume in reversed-phase HPLC. The correlation suggests that the hydrophobicity of the C-terminal amino acid is a major factor in governing the stability of the enzyme-substrate complex. The difference in the slope of the linear-regression lines seems to reflect the degree of relative hydrophobicity of the binding pockets in carboxypeptidase-Y and carboxypeptidase-A.