Investigating the Binding Dynamics and Stability of Bovine Serum Albumin with Antibiotics with Acridinedione Dye.

Exploring the energetics and bimolecular interaction of Bovine Serum Albumin (BSA) with various classes and generations of antibiotics in the absence and presence of a resorcinol based acridinedione dye (ADR1) were carried out. The binding stability of BSA-antibiotic complexes decreases on the introduction of ADR1 dye resulting in a positive value of free energy change, accompanied with several unfavourable interactions. Several polar amino acids contributed to the stability of the host-guest complex compared to that of non-polar amino acids, wherein BSA acts as the host, and antibiotics as the guest and ADR1 dye as the competing guest molecule. Hydrogen-bonding interactions govern the binding stability and energetics compared to that of hydrophobic interactions is elucidated in the present study.