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Title

INTERACTION OF ANTHRACYCLINE ANTIBIOTIC DAUNOMYCIN WITH HMGB1 AS NON-HISTONE PROTEIN IN SOLUTION

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 Start Page 198 | End Page 198

Abstract

 High mobility group (HMG) proteins are the most abundant group of CHROMATIN non-histone proteins. This family is composed of four major variants, including HMGB1, HMGB2, HMGB3 and HMGB4. As a highly evolutionary conserved protein, HMGB1 is the most studied and important member of this group. DAUNOMYCIN is a potent CHROMATIN-binding antitumor drug belonging to the family of anthracycline ANTITUMOR DRUGS. In this work, HMGB1 was purified from rat liver and incubated with various concentrations of DAUNOMYCIN and then its binding to DAUNOMYCIN was investigated, using equilibrium dialysis and circular dichroism spectroscopy techniques. The Scatchard plot obtained from the equilibrium dialysis study exhibited positive cooperative binding behavior and the occurrence of a negative Gibbs free energy (DGo = -6.57 Kcal/M), suggesting that the interaction process was exergonic. Association (Ka) and dissociation (Kd) constants were also determined (Ka: 7.71 ´ 104 M-1, Kd: 1.3 ´ 105 M). According to the circular dichroism data, upon addition of various concentrations of the drug, secondary structure of HMGB1 was altered in a dose dependent manner. Prediction of secondary structure of HMGB1 using relevant software showed that upon binding of DAUNOMYCIN to HMGB1 the alpha-helical content of the protein was increased. Summing up, the results suggest that DAUNOMYCIN binds to HMGB1 PROTEIN and this binding may influence HMGB1-DNA interaction followed by DNA-dependent activities of the protein in the cell.

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