Article ID Journal Published Year Pages File Type
1236508 Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy 2011 8 Pages PDF
Abstract

Various spectroscopy and molecular docking methods were used to examine the binding of Clozapine (CLZ) to human serum albumin (HSA) in this paper. By monitoring the intrinsic fluorescence of single Trp214 residue and performing Dansylamide (DNSA) displacement measurement, the specific binding of CLZ in the vicinity of Sudlow's Site I of HSA has been clarified. An apparent distance of 27.3 Å between the Trp214 and CLZ was obtained via fluorescence resonance energy transfer (FRET) method. In addition, the changes in the secondary structure of HSA after its complexation with CLZ ligand were studied with CD spectroscopy, which indicate that CLZ does not has remarkable effect on the structure of the protein. Moreover, thermal denaturation experiment shows that the HSA–CLZ complexes are conformationally more stable. Finally, the binding details between CLZ and HSA were further confirmed by molecular docking studies, which revealed that CLZ was bound at subdomain IIA through multiple interactions, such as hydrophobic effect, van der Waals forces and hydrogen bonding.

Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slideHighlights► Interation of Clozapine with HSA was studied. ► Using optical spectroscopy and molecular docking methods. ► The binding of Clozapine to HSA has not been reported. ► Clozapine binds at Sudlow's Site I of HSA.

Related Topics
Physical Sciences and Engineering Chemistry Analytical Chemistry
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