Mechanistic interaction studies of synthesized ZIF-8 nanoparticles with bovine serum albumin using spectroscopic and molecular docking approaches

Numerous studies have shown that nanosized zeolitic imidazolate framework particles (ZIF-8 NPs) serve as promising vehicles for pH-responsive drug delivery. An understanding of their interaction with serum proteins present in physiological systems will thus be of critical importance. In this work, monodisperse ZIF-8 NPs with an average size of 60 nm were synthesized at room temperature and characterized for their various physicochemical properties. Bovine serum albumin (BSA) was used as model serum protein for various interaction studies with ZIF-8 NPs. Spectroscopic techniques such as UV–visible and fluorescence spectroscopy indicated the formation of a ground-state complex with a binding constant of the order 10(3) M(−1) and a single binding site. Steady-state and time-resolved fluorescence spectroscopy confirmed the mechanism of quenching to be static. Conformational changes in the secondary structure of BSA were observed using CD and FT-IR spectroscopies. Binding sites were explored using molecular docking studies.