Spectroscopic and Molecular Docking Study of the Interaction between Neutral Re(I) Tetrazolate Complexes and Bovine Serum Albumin

Abstract Re(I) complexes have potential in biomedical sciences as imaging agents, diagnostics and therapeutics. Thus, it is crucial to understand how interact with carrier proteins, like serum albumins. Here, two neutral were used ( fac ‐[Re(CO) 3 (1,10‐phenanthroline)L], which L either 4‐cyanophenyltetrazolate (1) or 4‐methoxycarbonylphenyltetrazole ester (2) , study the interactions bovine albumin (BSA). Spectroscopic measurements, calculations of thermodynamic Förster resonance energy transfer parameters, well molecular modelling, performed differential binding between BSA complex 1 2 . Induced‐fit docking combined quantum‐polarised ligand employed what believed be a first for BSA. Our findings provide basis other interaction studies suggest that subtle functional group alterations at terminal region significant impact on ability this class compounds