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Initial evidence from UV-Vis absorption spectroscopy confirmed a ground-state complex formation between the drug and the protein. Subsequent fluorescence quenching studies established a static quenching mechanism, with a binding constant (Kb) of 3.99\u2009\u00d7\u200910\n                    <jats:sup>4<\/jats:sup>\n                    L\u00b7mol\n                    <jats:sup>\u22121<\/jats:sup>\n                    determined at 298\u00a0K, indicating moderate binding affinity. Analysis of the thermodynamic parameters, computed via the Van\u2019t Hoff equation, revealed that the binding process is both spontaneous and endothermic. The positive entropy change (\u0394S\u00b0) identified hydrophobic interactions as the predominant driving force for the complex formation.\n                  <\/jats:p>\n                  <jats:p>The binding site was precisely localized to subdomain IIA (Site I) of BSA, a finding consistently supported by two independent lines of evidence: competitive site-marker displacement assays and molecular docking simulations. Collectively, these insights into the binding affinity, forces, and specific location are fundamental for advancing the understanding of CFP\u2019s pharmacokinetic profile. 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