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7. Structural Dynamics of DPP-4 and Its Influence on the Projection of Bioactive Ligands.

Author

Pantaleão, Simone Queiroz, Philot, Eric Allison, de Resende-Lara, Pedro Túlio, Lima, Angélica Nakagawa, Perahia, David, Miteva, Maria Atanassova, Scott, Ana Ligia, and Honorio, Kathia Maria

Subjects
*CD26 antigen, *TYPE 2 diabetes treatment, *DRUG interactions, *MOLECULAR interactions, *MOLECULAR structure of enzymes
Abstract

Dipeptidyl peptidase-4 (DPP-4) is a target to treat type II diabetes mellitus. Therefore, it is important to understand the structural aspects of this enzyme and its interaction with drug candidates. This study involved molecular dynamics simulations, normal mode analysis, binding site detection and analysis of molecular interactions to understand the protein dynamics. We identified some DPP-4 functional motions contributing to the exposure of the binding sites and twist movements revealing how the two enzyme chains are interconnected in their bioactive form, which are defined as chains A (residues 40–767) and B (residues 40–767). By understanding the enzyme structure, its motions and the regions of its binding sites, it will be possible to contribute to the design of new DPP-4 inhibitors as drug candidates to treat diabetes. [ABSTRACT FROM AUTHOR]

Published
2018
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