Multi-spectral and docking assessments to explore the combination of an antiviral drug, entecavir with bovine serum albumin

• Published in: Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy Molecular and biomolecular spectroscopy, 2024-12, Vol.322, p.124792, Article 124792
• Main Authors: Murathan, Zeynep, Zahirul Kabir, Md, Seng, Jane, Mohamad, Saharuddin B., Uslu, Bengi
• Format: Article
• Language: English
• Subjects: Bovine serum albumin; Computational assessments; Entecavir; Fluorescence; Hepatitis B virus
• ISSN: 1386-1425
• DOI: 10.1016/j.saa.2024.124792

Binding Characteristics of ETV to BSA. [Display omitted] •ETV binds to BSA with a moderate binding strength.•ETV quenches the BSA fluorescence signal with a static nature.•Hydrogen bonds, van der Waals forces and hydrophobic interactions secure the ETV–BSA complex formation.•Interaction between ETV and BSA alters the protein’s molecular environment.•ETV favours to bind at site I of BSA. Molecular interaction of entecavir (ETV) with the transport protein, albumin from bovine serum (BSA) was explored through multispectral and molecular docking approaches. The BSA fluorescence was appreciably quenched upon ETV binding and the quenching nature was static. The ETV–BSA complexation and the static quenching process were further reiterated using UV–visible absorption spectra. The binding constant (Ka) values of the complex were found as 1.47 × 104–4.0 × 103 M−1, which depicting a modarate binding strength in the ETV–BSA complexation. The experimental outcomes verified that the stable complexation was primarily influenced by hydrophobic interactions, hydrogen bonds and van der Waals forces. Synchronous and 3-D fluorescence spectral results demonstrated that ETV had significant impact on the hydrophobicity and polarity of the molecular environment near Tyr and Trp residues. Competitive site-markers displacement (with warfarin and ketoprofen) results discovered the suitable binding locus of ETV at site I in BSA. The molecular docking assessments also revealed that ETV formed hydrogen bonds and hydrophobic interactions with BSA, predominantly binding to site I (sub-domain IIA) of BSA.