Investigating the binding affinities of fructose and galactose to human serum albumin: simulation studies

Human serum albumin (HSA) is abundant in blood. HSA binds a wide range of drugs, metabolites, and nutrients. A glycated also potential diabetes biomarker. Recently, crystal structures glucose- fructose-bound have been reported. Both cyclic acyclic sugar forms are trapped Sudlow site I. Galactose can bind HSA, but no atomic detail available. Thus, molecular dynamics simulations were employed to study the structural dynamic properties fructose- galactose-bound comparison glucose-bound from previous studies. bound sugars promote different degrees domain motions which affect drug/solute binding affinity at large highly water-exposed I allows high mobility sugars. Nonetheless, more protein contacts imply tighter fructose than galactose. Although galactose glucose epimers, interaction network disrupts formation interactions with K195 K199 resulting escape In contrast, molecules anchored inside by number dimer structure. These highlights importance protein–sugar sugar–sugar for ligand cavity.