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E. M. Kirilin, V. K. Švedas
Study of the
conformational variety of the oligosaccharide substrates of neuraminidases from
pathogens using molecular modeling
Abstract
Analysis of the
conformational variety of the oligosaccharide fragments of the human glycan
receptors LSTa (α-D-Neu5Ac-(2-3)-β-D-Gal-(1-3)-β-D-GlcNAc-(1-3)-β-D-Gal(1-4)-D-Glc) and LSTc(α-D-Neu5Ac-(2-6)-β-D-Gal-(1-3)-β-D-GlcNAc-(1-3)-β-D-Gal(1-4)-D-Glc) in aqueous solution has been performed with the
comprehensive use of molecular modeling and statistical data processing
followed by determination of major and minor stabilized conformers and
selection of relevant topologies. The sialic acid ring conformational free
energy landscape for both pentasaccharides has been reconstructed and analyzed
giving a specification of the most probable distorted ring conformations of the
basic chair 1C4 structure. The obtained results are in a good agreement with
experimental data generated by nuclear magnetic resonance spectroscopy and
x-ray crystallography.
Key words:
sialoglycans conformations, molecular modeling, metadynamics.
Copyright (C) Chemistry Dept., Moscow State University, 2002
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