110755-29-8

Upstream product

• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 107-85-7 1-amino-3-methylbutane 
• 41518-17-6 Z-Phe-O-COO-isoBu 
• 1161-13-3 N-Cbz-L-Phe 
• 3674-06-4 Boc-Phe-ONSu 
• 110755-28-7 N-carbobenzyloxy-L-phenylalanine isopentylamide 

Downstream Products

• 1283077-15-5 C₂₃H₂₆ClN₃O₂ 
• 887255-59-6 [1-(3-methyl-butylcarbamoyl)-2-phenyl-ethyl]-carbamic acid 1,1-dioxo-1H-1λ⁶-benzo[b]thiophen-2-ylmethyl ester 

Relevant academic research and scientific papers

Design, synthesis and evaluation of 3-methylene-substituted indolinones as antimalarials

The design, synthesis and evaluation of 3-methylene-substituted indolinones as falcipain inhibitors and antiplasmodial agents are described. These compounds react readily with thiols via an addition-elimination mechanism, indicating their potential as cys

The Bsmoc group as a novel scaffold for the design of irreversible inhibitors of cysteine proteases

Carbamate and ester derivatives of the 1,1-dioxobenzo[b]thiophen-2-ylmethyloxycarbonyl (Bsmoc) scaffold react readily with thiols via a Michael addition at rates not significantly affected by the nature of the carboxylic or carbamic acid leaving group. These Michael acceptors are irreversible inhibitors of the cysteine proteases papain and human liver cathepsin B, displaying first-order kinetics with respect to inhibitor concentration. In contrast, none of the Bsmoc derivatives inhibited porcine pancreatic elastase, a serine protease.

N-Haloacetyl-amino-acid amides as active-site-directed inhibitors of papain and cathepsin B

A series of N-haloacetyl-amino-acid amides were synthesized and tested as models of cysteine-protease inhibitors. They irreversibly inactivated papain and cathepsin B via a reversible enzyme-inhibitor intermediate. Apparent second-order rate constants of inactivation ranging from 65 to 16,700 M-1 s-1 were observed. Reactivity against papain, as compared to glutathione, was increased 16,400-fold for N-bromoacetyl-leucine isopentylamide and 25,700-fold for the corresponding iodoacetyl derivative; these increases are probably due to proximity effects. No inhibition of trypsin, chymotrypsin and porcine pancreatic elastase was observed. Haloacetamides represent an interesting class of easily synthesized, efficient, irreversible inhibitors of cysteine proteases, which have low non-specific alkylating properties.