Spectroscopic and in silico evaluation on the interactive behavior between substituted β-2,3-dihydrofuran naphthoquinones and human serum albumin

•The binding HSA:β−2,3-dihydrofuran naphthoquinones 1–5 is moderate in the ground-state.•Subdomain IIA, where Trp-214 residue can be found, is the main binding site.•The binding is both entropically and enthalpically driven stabilized by hydrophobic, hydrogen bond, and electrostatic interactions.•The obtained binding affinity for HSA:1,2-naphthoquinones are like those reported for HSA:1,4-naphthoquinones.