19391-50-5

Upstream product

• 1161-13-3 N-Cbz-L-Phe 
• 1080-06-4 L-Tyr-OMe 
• 3417-91-2 L-tyrosine methyl ester HCl 
• 501-53-1 benzyl chloroformate 
• 60-18-4 L-tyrosine 
• 63-91-2 L-phenylalanine 
• 37535-70-9 Z-Phe-4-nitroguaiacylester 
• 3397-32-8 N-(benzyloxycarbonyl)-phenylalanine-N-hydroxysuccinimide ester 

Downstream Products

• 60142-81-6 H-Tyr-Phe-OMe*HCl 
• 2537-91-9 N-benzyloxycarbonyl-L-phenylalanyl-L-tyrosine 
• 19777-77-6 N-(N-Benzyloxycarbonyl-L-phenylalanyl)-L-tyrosin-hydrazid 

Relevant academic research and scientific papers

Synthesis, bioactivity, docking and molecular dynamics studies of furan-based peptides as 20s proteasome inhibitors

Proteasome inhibitors are promising compounds for a number of therapies, including cardiovascular and eye diseases, diabetes, and cancers. We previously reported a series of furanbased peptidic inhibitors with moderate potencies against the proteasome b5 subunit, hypothesizing that the C-terminal furyl ketone motif could form a covalent bond with the catalytic residue, threonine 1. In this context, we describe further optimizations of the furan-based peptides, and a series of dipeptidic and tripeptidic inhibitors were designed and synthesized, aiming at improved potency and better solubility. Most of the tripeptidic inhibitors demonstrated improved potency and selectivity as b5 subunit inhibitors in both enzymatic and cellular assays, and good antineoplastic activities in various tumor cell lines were also observed. However, no inhibitory effects were observed for the dipeptidic compounds, which led us to presume that a noncovalent binding mode is adopted. Docking studies and molecular dynamics simulations were carried out to verify this presumption, with results showing that the distance between the furyl ketone motif and Thr1 is slightly too long to form covalent bond.

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.

6-Nitro-1-β-Naphthalenesulfonyloxybenzotriazole : A Novel Coupling Reagent For Peptide Synthesis

Synthesis of 6-nitro-1-β-naphthalenesulfonyloxybenzotriazole (N-NSBt) and its application as a peptide coupling ragent is being reported.It has been found to be suitable for rapid and quantitative synthesis of optically pure peptides in a stepwise manner.

Chlorosulfite, a Versatile and Mild Condensation Reagent for the Synthesis of Peptides

The title compound 5, which can be easily obtained from hexamethylphosphoric triamide (1) and thionyl chloride by catalysis of dimethylformamide, is succesfully applied as a mild condensation reagent for the synthesis of peptides.