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The interaction of dothiepin (DOT) and doxepin (DOX) with bovine serum albumin (BSA) and a DNA base (adenine) was studied using UV-visible, fluorescence, attenuated total reflection-infra-red (ATR-IR), cyclic voltammetry and molecular docking methods. Strong fluorescence quenching was observed upon interaction of DOT and DOX with BSA/adenine and the mechanism suggested static quenching. Hydrophobic and hydrogen bonding interactions were the predominant intermolecular forces needed to stabilize the copolymer. Upon addition of the drugs: (i) the tautomeric equilibrium structure of the adenine was changed; and (ii) the oxidation and the reduction peaks of the adenine/BSA interaction shifted towards high and low potentials, respectively. In ATR-IR, the band shift of amides I and II indicated a change in secondary structure of BSA upon binding to DOT and DOX drugs. The reduction in voltammetric current in the presence of BSA/adenine was attributed to slow diffusion of BSA/adenine binding with DOX/DOT. The docking method indicated that the drug moiety interacted with the BSA molecule. Copyright © 2016 John Wiley & Sons, Ltd.

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ABSTRACT. Quenching of bovine serum albumin (BSA) and DNA base (adenine) by sulfamerazine (SM) and sulfamethazine (SMT) was studied using UV-visible, fluorescence cyclic voltammetry and molecular docking methods. A strong fluorescence quenching reaction of SM and SMT to BSA/adenine was observed and the quenching mechanism was suggested as static. Both drugs can bind to BSA and adenine with stoichiometric ratio of 1:1 and the protein -drug complexes are stabilized mainly by hydrogen bonds and van der Waals interaction. Compared to SM, SMT contributes substantially higher binding efficiency with BSA/adenine. With addition of drug solution to the adenine/BSA, the oxidation and the reduction peaks shifted towards high and low potentials, respectively. R o , J, r and E values in the BSA-drugs are higher than that of adeninedrug molecules suggest that binding of the sulfa drugs with BSA is higher than adenine -drug molecules. Docking method specify that bioactive site of sulfa drugs moiety, the aniline group is interacted with the BSA molecules.