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model-based approach for investigating the interaction of the antibiotic imipenem with a series of human serum albumin mutants. We report a computational modelling study of the inhibition of imipenem by human serum albumin (HSA) and HSA variants, based on the direct binding of imipenem to HSA and an assumed reversible one-step binding mechanism. Models were constructed with thedocking software FRED in both the closed and open form of HSA, and the subsequent effect of mutants on HSA conformation, ligand binding, and associated protein stability was investigated. Model predictions were compared to experimental data for n(S-1)-alkyl-p-nitroanilides and 1-amino-2-ethoxy-propane-1-sulfonic acid. The analysis suggests that imipenem binding to the closed protein
structure produces a higher inhibitory efficiency than its binding to the open protein conformation. The substitution of His404, the only amino acid in HSA which exhibits different structural characteristics in the closed versus the open protein conformation, strongly increases the stability and availability of the binding site for imipenem. This is demonstrated by the opposite effects of His404
substitution on the association rate and the dissociation rate of imipenem from the protein. The half-site maximal binding potential of HSA (K(i,half)) was estimated to be 17 +/- 4 microM for the closed protein conformation and 43 +/- 4 microM for the open conformation. It is likely that this estimation is underestimated because of the large aggregation of HSA when it is docked in the closedconformation. Among the isolated HSADownload

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