ArticleMolecules (Basel, Switzerland)2025
The Molecular Recognition of Lurasidone by Human Serum Albumin: A Combined Experimental and Computational Approach.
Article in Molecules (Basel, Switzerland), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
What it found
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Who cites it
3 citing papers in PubMed.
- Palladium(II) Complexes with Chloro-Substituted Salicyl Schiff Bases: Exploring Multimodal Anticancer Mechanisms and Catalase Inhibition.Molecules (Basel, Switzerland) · 2026Article
- Unveiling the Bio-Interface via Spectroscopic and Computational Studies of (Propyl-3-ol/butyl-4-ol)triphenyltin(IV) Compound Binding to Human Serum Transferrin.Materials (Basel, Switzerland) · 2026Article
- Review of Autism Spectrum Disorder (ASD): Epidemiology, Aetiology, Pathology, and Pharmacological Treatment.Pharmaceuticals (Basel, Switzerland) · 2025Review
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lurasidone (LUR) is an antipsychotic drug whose interaction with human serum albumin (HSA) plays a crucial role in its pharmacokinetic and pharmacodynamic properties. A thorough understanding of LUR's binding mechanism to HSA is crucial for predicting its transport, distribution, and potential drug interactions.
methodsThe interaction between LUR and HSA was investigated using fluorescence and circular dichroism (CD) spectroscopy, followed by molecular docking simulations. Binding characteristics were analyzed through quenching mechanisms, thermodynamic parameters, and competitive site marker experiments.
resultsThis study revealed a systematic decrease in HSA fluorescence intensity with increasing LUR concentration, indicating a static quenching mechanism driven by non-fluorescent complex formation. Binding constants suggest enhanced complex stability at higher temperatures, with thermodynamic analysis confirming an endothermic, hydrophobic interaction. Competitive site marker assays and synchronous fluorescence spectra confirmed that LUR primarily binds to site I (subdomain IIA) near tryptophan residues. Conformational changes in HSA, observed as a decrease in α-helix content, further demonstrate the structural impact of LUR binding.
conclusionsThese findings offer key insights into the molecular interactions between LUR and HSA, enhancing our understanding of LUR's pharmacokinetics and its potential interactions with other drugs. Understanding these binding characteristics can aid in optimizing LUR's clinical application and predicting possible interactions with other biomolecules.
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