Reversible inhibition of cathepsin L-like proteases by 4-mer pseudopeptides

Add time:08/15/2019    Source:sciencedirect.com

A library of 121 pseudopeptides was designed to develop reversible inhibitors of trypanosomal enzymes (cruzain from Trypanosoma cruzi and congopain from Trypanosoma congolense). The peptides share the framework: Cha-X1-X2-Pro (Cha=cyclohexyl-alanine, X1 and X2 were phenylalanyl analogs), based on a previous report [Lecaille, F., Authié, E., Moreau, T., Serveau, C., Gauthier, F. and Lalmanach, G. (2001) Eur. J. Biochem. 268, 2733–2741]. Five peptides containing a nitro-substituted aromatic residue (Tyr/Phe) and one a 4-chloro-phenylalanine at the X1 position, and 3-(2-naphthyl)-alanine, homocyclohexylalanine or 3-nitro-tyrosine (3-NO2-Tyr) at the X2 position, were selected. They inhibited congopain more effectively than cruzain, except Cha-4-NO2-Phe-3-NO2-Tyr-Pro which bound the two parasitic enzymes similarly. Among this series, Cha-3-NO2-Tyr-HoCha-Pro and Cha-4-NO2-Phe-3-NO2-Tyr-Pro are the most selective for congopain relative to host cathepsins. No hydrolysis occurred upon prolonged incubation time with purified enzymes. In addition introduction of non-proteogenic residues in the peptidyl backbone greatly enhanced resistance to proteolysis by mammalian sera.

We also recommend Trading Suppliers and Manufacturers of L-Homocyclohexyl alanine (cas 116622-38-9). Pls Click Website Link as below: cas 116622-38-9 suppliers

Prev:Contributed paperMicrobial synthesis of (+) and (−) methyl 4-chloro-4,4-difluoro-3-hydroxybutanoate
Next:Full Length ArticleIn vitro studies of the antileishmanial activity of the newer 2-(substitutedphenoxy)-N-[(aryl)methylidene]acetohydrazide analogues)