Insights into the Binding of Cafaminol to Human Serum Albumin: Multi-Spectroscopic and Molecular Modeling Studies

In this study, the binding affinity of Cafaminol with humanserum albumin (HSA) was investigated by fluorescence, UV, and circular dichroism (CD) spectroscopies, along with molecular dynamics and Docking simulations. The Stern- Volmer plots were employed to specify the fluorescence quenching mechanism, while the simulation methods were utilized to deduce the approximate binding position of cafaminol on HSA. On the other hand, thermodynamic parameters, enthalpy and entropy changes, were determined using the Vant Hoff equation and analyzed to specify the main acting forces, between cafaminol and HSA. The overall results showed that cafaminol was bound to the domain IA of HSA, as a result of an enthalpy-driven process, mainly through the van der Waals and hydrogen bonding interactions. Static quenching mechanism was found to be responsible for the fluorescence quenching of HSA in the cafaminol presence, while the number of binding sites, and apparent binding constant were measured accordingly