tailieunhanh - Báo cáo khoa học: Thermodynamic analysis of porphyrin binding to Momordica charantia (bitter gourd) lectin

Owing to theuseof porphyrins inphotodynamic therapy for the treatment of malignant tumors, and the preferential interaction of lectins with tumor cells, studies on lectin– porphyrin interactionareof significant interest. In this study, the interaction of several free-base and metalloporphyrins withMomordica charantia(bitter gourd) lectin (MCL) was investigated by absorption spectroscopy. Difference absorp-tion spectra revealed that significant changes occur in the Soret band region of the porphyrins on binding to MCL | Eur. J. Biochem. 271 3274-3282 2004 FEBS 2004 doi Thermodynamic analysis of porphyrin binding to Momordica charantia bitter gourd lectin Nabil A. M. Sultan Bhaskar G. Maiya and Musti J. Swamy School of Chemistry University of Hyderabad India Owing to the use of porphyrins in photodynamic therapy for the treatment of malignant tumors and the preferential interaction of lectins with tumor cells studies on lectin-porphyrin interaction are of significant interest. In this study the interaction of several free-base and metalloporphyrins with Momordica charantia bitter gourd lectin MCL was investigated by absorption spectroscopy. Difference absorption spectra revealed that significant changes occur in the Soret band region of the porphyrins on binding to MCL. These changes were monitored to obtain association constants Ka and stoichiometry of binding. The tetrameric MCL binds four porphyrin molecules and the stoichiometry was unaffected by the presence of the specific sugar lactose. In addition the agglutination activity of MCL was unaffected by the presence of the porphyrins used in this study clearly indicating that porphyrin and carbohydrate ligands bind at different sites. Both cationic and anionic porphyrins bind to the lectin with comparable affinity Ka 103-105 M 1 . The thermodynamic parameters associated with the interaction of several porphyrins obtained from the temperature dependence of the Ka values were found to be in the range AH to kJ-mol-1 and AS to J-mol-1-K-1. These results indicate that porphyrin binding to MCL is governed by enthalpic forces and that the contribution from binding entropy is negative. Enthalpy-entropy compensation was observed in the interaction of different porphyrins with MCL underscoring the role of water structure in the overall binding process. Analysis of CD spectra of MCL indicates that this protein contains about 13 a-helix 36 b-sheet 21 b-turn and the rest unordered .