South Asian Journal of Life Sciences

Research Article
S. Asian J. Life Sci. 4(1): 32- 39
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Hung Nguyen1, Thu Nguyen1, Ly Le1, 2* 

1Life Science Laboratory, Institute for Computational Science and Technology, Ho Chi Minh City, Vietnam; 2School of Biotechnology, Ho Chi Minh International University, Vietnam National University, Vietnam.

Abstract | The aim of this work is to use molecular dynamics simulation to study the influence of mutated residues in interaction between G6P substrate-NADP+ coenzymes and Glucose-6-phosphate-dehydrogenase (G6PD) enzyme for wild type and three mutants (Vancouver, Wayne and Aachen mutants). The binding free energy (calculated by molecular mechanic Poisson-Boltzmann surface area (MM-PBSA) method) and hydrogen bond values between G6P substrate-NADP+ coenzymes and G6PD enzymes are identified as important in mutated residues to thermodynamic mechanism of G6PD enzyme in protecting the cells against oxidative stress and protective against malaria and this may assist further experimental study and strategies for rational design of new inhibitors.

Keywords | G6PD enzyme; G6P substrate-NADP+ coenzymes; wild type; Wayne, Aachen and Vancouver mutants; MM-PBSA method