Molecular insights into nilvadipine-hemoglobin interactions: conformational dynamics and binding mechanisms.

ABSTRACT: Understanding the molecular basis of drug-protein interactions is essential for predicting pharmacokinetics and potential off-target effects. Here, we employ a combined experimental and computational approach to characterize the binding of Nilvadipine (a dihydropyridine calcium channel blocker) to hemoglobin (Hb). Using Soret band absorption and steady-state fluorescence spectroscopy across 298-310 K, we observed pronounced static quenching of Hb's intrinsic fluorescence, yielding Stern-Volmer constants (K _SV) in the order of 10⁴ M^-1 and 1 : 1 binding stoichiometry. Thermodynamic parameters derived from van't Hoff analysis (ΔH° > 0, ΔS° > 0, and ΔG° < 0) highlighted hydrophobic interactions as the primary driving force and confir

SUBMITTER: Khan MS 

PROVIDER: S-EPMC12604001 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature