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Updated: Sep 15, 2025
Incorporating Target Protein Structure Flexibility and Dynamics in Computational Drug Discovery Using Ensemble-Based Docking Analysis
Published on: June 20, 2025
Glycated human serum albumin: Computational studies of drug binding through molecular docking and binding affinity
Laurent Soulère1, Christophe O Soulage2
1INSA Lyon, Universite Claude Bernard Lyon 1, CNRS, CPE-Lyon, ICBMS, UMR 5246, Institut de Chimie et de Biochimie Moléculaires et Supramoléculaires, Bâtiment Lederer, 1 Rue Victor Grignard, Villeurbanne F-69622, France.
Abstract:
Human serum albumin (HSA) plays a major role in the transport of endogenous and exogenous compounds such as many drugs and thus in the distribution of these essential molecules towards tissues and organs. The glycation of HSA can easily be formed either in normal or diabetic conditions, perturbating the function of this key protein. In this work, we developed a method aiming at estimating the relative binding affinities for glycated and normal HSA at the Sudlow site I which is the most sensitive to protein glycation due to Lys195 glycation. This method involves molecular docking and affinity prediction and was exemplified for several common drugs with available structure in complex with HSA and extended to three other drugs involved in the treatment of diabetes without structural data.
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