@Article{JAMS-8-3,
author = {Yan, Fangfang and Xinguo, Liu and Zhang, Shaolong and Su, Jing and Zhang, Qinggang and Jianzhong, Chen},
title = {Binding Difference of Inhibitors ACD and TDZ to A-FABP Revealed by Molecular Dynamics Simulations},
journal = {Journal of Atomic and Molecular Sciences},
year = {2017},
volume = {8},
number = {3},
pages = {97--104},
abstract = {<p style="text-align: justify;">Adipocyte fatty-acid binding protein (A-FABP) is abundantly expressed in macrophage and adipocyte, and it is a potential target for the treatment of atherosclerosis and metabolic disease. In this work, binding differences of two inhibitors ACD and TDZ to A-FABP were studied by using principal component (PC) analysis, molecular mechanics generalized Born surface area (MM-GBSA) and solvated interaction energy (SIE) methods. The results show that the binding of inhibitor TDZ to A-FABP is stronger than that of ACD to A-FABP. The calculation of residue-based free energy decomposition and dynamics analysis of hydrogen bonds suggest that hydrophobic interactions and hydrogen bonding interactions play important roles in the structural stability of A-FABP. The information obtained from this work will provide a useful clue for design of effective drugs targeting A-FABP.&nbsp;</p>},
issn = {2079-7346},
doi = {https://doi.org/10.4208/jams.110417.121517a},
url = {https://global-sci.com/article/74212/binding-difference-of-inhibitors-acd-and-tdz-to-a-fabp-revealed-by-molecular-dynamics-simulations}
}