N-Lipidated Amino Acids and Peptides Immobilizedon Cellulose Able to Split Amide Bonds.

ABSTRACT: N-lipidated short peptides and amino acids immobilized on the cellulose were used ascatalysts cleaved amide bonds under biomimetic conditions. In order to select catalytically mostactive derivatives a library of 156 N-lipidated amino acids, dipeptides and tripeptides immobilizedon cellulose was obtained. The library was synthesized from serine, histidine and glutamic acidpeptides N-acylated with heptanoic, octanoic, hexadecanoic and (E)-octadec-9-enoic acids.Catalytic efficiency was monitored by spectrophotometric determination of p-nitroaniline formedby the hydrolysis of a 0.1 M solution of Z-Leu-NP. The most active 8 structures contained tripeptidefragment with 1-3 serine residues. It has been found that incorporation of metal ions into catalyticpockets increase the activity of the synzy

SUBMITTER: Fraczyk J 

PROVIDER: S-EPMC6416662 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature