Characterization of Climbazole-Bovine serum albumin interaction by experimental and in silico approaches.

Interactive association of an antifungal drug, climbazole (CBZ) with the carrier protein in bovine circulation, bovine serum albumin (BSA) was explored by fluorescence and absorption spectroscopy along with in silico techniques. The fluorescence and absorption spectral alterations of the protein upon addition of CBZ affirmed the complex foration between CBZ and BSA. The inverse temperature dependence behaviour of the K values as well as the hyperchromic result of the protein's absorption signals characterized CBZ-triggered quenching of BSA fluorescence as the static quenching.

Spectrofluorometric and computational approaches for the interaction studies of aclonifen and bifenox with human serum albumin.

Interaction of two broadly used herbicides, aclonifen (ACF) and bifenox (BIF) with the major transporter in human circulation, human serum albumin (HSA) were examined using fluorescence and absorption spectral measurements combined with in silico analyses. Assessment of the fluorescence and absorption spectral results affirmed the complexation between ACF/BIF and HSA. Increase in the K value with temperature characterized the ACF/BIF-induced quenching of the protein fluorescence as dynamic quenching.