ABSTRACT In the current study, we have designed three hitherto unreported, aldimine‐based zinc complexes, used as precursors to prepare the corresponding zinc oxide nanomaterials. The complexes are further assessed for binding propensity with BSA and human serum albumin (HSA), the homologous proteins. The interactions with plasma proteins indicate the drug‐like behaviour of the complexes and play a significant role in drug design and pharmacology research. Both proteins possess typical physicochemical properties and functions, acting as drug carriers in plasma. UV absorption titration and fluorescence quenching studies have been used to investigate the interaction of zinc complexes with both proteins. From the results, it has been observed that the ZnHL3 complex shows higher binding constants than the other complexes. Drug loading is a promising approach for developing amorphous pharmaceuticals that are highly stable and have enhanced bioavailability, solubility, and dissolution rates. Hence, we have assessed the relative curcumin loading abilities of complex/nanomaterial‐coated BSA.
Sekar et al. (Sun,) studied this question.