부산대학교 도서관

The investigation of the binding between isoniazid (or isonicotinic acid hydrazide, INH) and serum albumin is of crucial importance to reveal the reason of resistant Mycobacterium tuberculosis strains towards INH and to increase the anti-tuberculous activity of INH. The interaction between INH and bovine serum albumin (BSA) was studied by fluorescence, UV and FT-IR spectroscopy methods. The analysis of the emission quenching at different temperatures revealed that the quenching mechanism corresponds to a static process and, as consequence; a complex INH–BSA is formed. The modified Stern–Volmer quenching constant Ka and the corresponding thermodynamic parameters ΔH, ΔG and ΔS were calculated. The distance, r, between donor (BSA) and acceptor (INH) was calculated to be 2.14 nm based on Förster’s non-radiative energy transfer theory (FRET). The results obtained on the basis of fluorescence study of BSA solutions at the presence of dimethylsulfoxide (DMSO) were discussed in terms of the hydration properties and competitive intermolecular interactions between BSA and solvent components. The dependence of binding constant on the concentration of added DMSO as a solvent component showed non monotonous behavior. The conformational changes of BSA and its secondary structure alterations at the presence of INH were revealed.