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A. D. Ilyina, D. Ibarra-Coronado, K. Gurumurthy, F. Cerda-Ramarez
Evidence of catalytic
activity of polypeptides artificially synthesized from conservative
aminoacids
Abstract
The objectives of this study were to obtain the
combinatorial libraries in water and reverse micellar systems and to evaluate
their catalytic activity applying the reverse micelles as micro-reactors
defined the restrictions of size and conformation. The amino acids, viz., Gly,
Asp, His, Arg and Leu were selected for polypeptide synthesis based on the
reported bioinformatic approaches. The polypeptides were synthesized by
carbodiimide method. The activity was defined as increase in absorbance after
15 min of reaction with reference to control without amino acids using ABTS,
catechol, pyrogallol as the substrates for oxidase activity, ABTS/H2O2 as the substrates for peroxidase activity
and NIPAB as the substrate for hydrolase activity, with and without Zn2+,
Cu2+, Mn2+ sulfates
and hemin. The evidence of catalytic activity was observed in the synthesized
combinatorial libraries. The presence of polypeptide chains was demonstrated by
electrophoresis.
Copyright (C) Chemistry Dept., Moscow State University, 2002
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