albumin - publications

Predict more albumin - ligand interactions now!


1. Mol Biol Rep. 2012 Feb 12. [Epub ahead of print]

Study on the interaction between isoniazid and bovine serum albumin by
fluorescence spectroscopy: the effect of dimethylsulfoxide.

Markarian SA, Aznauryan MG.

Department of Chemistry, Yerevan State University, 0025, Yerevan, Armenia,
shmarkar@ysu.am.

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 K (a) 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.

PMID: 22327779 [PubMed - as supplied by publisher]