Abstract
Diabetes mellitus is one of the most common diseases in the world. Currently around 3% of the global population suffers from diabetes and this is expected to double by 2030. During hyperglycemic episodes, protein glycation may occur on lysine residues. Decrease of biological activity as a direct effect of glycation has been shown on calmodulin, superoxide dismutase and calcium ATPase on human erythrocytes. In this work, we evaluated the structural and dynamical effects due to lysine glycation on human acetylcholinesterase and butyrylcholinesterase. Four probable sites were tested and analyzed for each cholinesterase by molecular dynamics simulations, using the CHARMM27 forcefield in NAMD at 298K, for 25ns on each model. The cumulative effect of each site was studied comparing it to the native, unglycated protein structure. The structural and dynamic consequences due to lysine glycation on the conformation of the choline binding site are reported.Funding: Macroproyecto de Tecnologias de la Informacion y la Computacion (UNAM), Centro Nacional de Supercomputo (IPICYT), Supercomputadora Aitzaloa (UAM). Postdoctoral Funding (CONACYT).
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