Shiraz University Press Molecular Biology Research Communications 2322-181X 1 2 2013 01 05 Molecular dynamics simulation and docking studies on the binding properties of several anticancer drugs to human serum albumin 65 73 628 10.22099/mbrc.2013.628 EN Fatemeh Keshavarz Department of Chemistry, Shiraz University of Technology, Shiraz 71555-313, Iran Mohammad Mehdi Alavianmehr Department of Chemistry, Shiraz University of Technology, Shiraz 71555-313, Iran. Reza Yousefi Protein Chemistry Laboratory (PCL), Department of Biology, Shiraz University, Shiraz 71454, Iran. Journal Article 2012 11 18 Disposition and transportation of anticancer drugs by human serum albumin (HSA) affects their bioavailability, distribution and elimination. In this study, the interaction of a set of anticancer drugs with HSA was investigated by molecular dynamics and molecular docking simulations. The drugs' activities were analyzed according to their docking scores, binding sites and structural descriptors. The results displayed the ability of cavity 1, located in the cleft between domains I and III, to potentiate as the principal binding site of all tested drugs. This cavity provides a large space without any effective steric hindrance and induces the stability of the drugs in their binding sites by short and long ranged interactions with the accessible residues. Yet, specific structural features may lead some drug configurations to advance stronger interactions with cavities other than cavity 1. Also, the small volume and position of some cavities i.e. cavities 3, 5-10 involve penetration, small molecular volume and specific geometry which consequently force most drugs out of the corresponding binding sites.  Therefore, the steric factor seems to play the most important role in the transportation of drugs by HSA. https://mbrc.shirazu.ac.ir/article_628_51277fb4268216f31896758766803921.pdf