4.6 Article

A Comprehensive Investigation of Interactions between Antipsychotic Drug Quetiapine and Human Serum Albumin Using Multi-Spectroscopic, Biochemical, and Molecular Modeling Approaches

Journal

MOLECULES
Volume 27, Issue 8, Pages -

Publisher

MDPI
DOI: 10.3390/molecules27082589

Keywords

quetiapine; human serum albumin; hydrophobic interaction; thermodynamic parameters

Funding

  1. King Saud University, Riyadh, Saudi Arabia [RSP-2021/357]

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This study investigates the interactions and binding mechanism between quetiapine (QTP) and human serum albumin (HSA) using spectroscopic and molecular docking techniques. The experimental results suggest the formation of a complex between QTP and HSA, with the involvement of hydrophobic forces. The study sheds light on the transport and delivery mechanism of QTP via HSA, and may contribute to the design of more effective QTP derivatives.
Quetiapine (QTP) is a short-acting atypical antipsychotic drug that treats schizophrenia or manic episodes of bipolar disorder. Human serum albumin (HSA) is an essential transport protein that transports hormones and various other ligands to their intended site of action. The interactions of QTP with HSA and their binding mechanism in the HSA-QTP system was studied using spectroscopic and molecular docking techniques. The UV-Vis absorption study shows hyperchromicity in the spectra of HSA on the addition of QTP, suggesting the complex formation and interactions between QTP and HSA. The results of intrinsic fluorescence indicate that QTP quenched the fluorescence of HSA and confirmed the complex formation between HSA and QTP, and this quenching mechanism was a static one. Thermodynamic analysis of the HSA-QTP system confirms the involvement of hydrophobic forces, and this complex formation is spontaneous. The competitive displacement and molecular docking experiments demonstrated that QTP is preferentially bound to HSA subdomain IB. Furthermore, the CD experiment results showed conformational changes in the HSA-QTP system. Besides this, the addition of QTP does not affect the esterase-like activity of HSA. This study will help further understand the credible mechanism of transport and delivery of QTP via HSA and design new QTP-based derivatives with greater efficacy.

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