MOLECULAR DYNAMICS OF THE STRUCTURAL COMPLEX OF THE HIV-1 GP41 PROTEIN WITH MONOCLONAL ANTIBODY 10E8 EXHIBITING BROAD VIRAL NEUTRALIZATION
Abstract
Conformational and energy characteristics of the structural complex between the HIV-1 gp41 protein and monoclonal antibody 10e8 exhibiting broad viral neutralization were studied by molecular dynamics simulations. Contributions of the amino acid residues of the gp41 protein and antibody 10e8 to the enthalpy constituent of the free energy of the complex formation were estimated. Residues Tyr- 99, Asp-100, Phe-100a, Trp-100b of the heavy chain of antibody 10e8 and Trp-672, Phe-673, Arg-683 of the gp41 protein were shown to be critical for the binding. The results obtained form a productive basis for virtual screening, computer testing, and development of novel HIV-1 entry inhibitors presenting the antibody 10e8 peptidomimetics with broad-spectrum neutralizing activity.
About the Authors
I. A. KASHYN
Институт биоорганической химии НАН Беларуси, Минск
Belarus
Belarus
A. V. TUZIKOV
Объединенный институт проблем информатики НАН Беларуси, Минск
Belarus
Belarus
A. M. ANDRIANOV
Институт биоорганической химии НАН Беларуси, Минск
Belarus
Belarus
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