Linamarin Binding to Human Serum Albumin. A Spectroscopic and Molecular Docking Approach

Abstract The interaction between linamarin (LIN), a cyanogenic glycoside, and human serum albumin (HSA) was studied by multiple spectroscopic techniques and molecular docking simulation. All measurements were performed under physiological conditions. The obtained results (including the binding constants, effective quenching constant and a number of binding sites) showed that the complex of HSA‐LIN is formed. The values of Stern‐Volmer constants (6.70×10 3 , 5.53×10 3 and 1.95×10 3 ) indicate that fluorescence quenching of HSA was static. Results of site marker experiments showed that the binding site of LIN is mainly located in site I (subdomain IIA) of HSA. The thermodynamic parameters showed that binding process occurs spontaneously through hydrophobic interactions. Molecular docking results are in good agreement with experimental data. Furthermore, computational results revealed LIN binds in the cavity of TRP 214, that is, subdomain IIA (site I) of HSA. This comprehensive study provides a deeper insight into ligand binding in HSA which may be useful in drug design and pharmacology.