Abstract
An optical biosensor with a stirred cuvette has been used to monitor the interaction of immobilized wheat germ agglutinin (WGA) with two water-soluble cationic porphyrins. The association constants (K a) of the free base porphyrin and its Zn(II) complex form were 2.66 and 27.31×105 L/mol at 20°C respectively. The interactions of the free base porphyrin were further investigated at temperatures between 15°C and 37°C. The thermodynamics parameters, changes in free energy, enthalpy and entropy, were −31.23, 22.92, 54.15 kJ/mol respectively. The heat capacity change was −355.53 J·mol−1·K−1. The binding was driven by entropic contribution, and showed strong enthalpy-entropy compensation. It was governed primarily by hydrophobic forces.
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Foundation item: Supported by the National Natural Science Foundation of China (30370366)
Biography: QIN Yimin (1976-), female, Ph. D., research direction: applied biochemistry and molecular biology.
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Yimin, Q., Nina, P. & Guolin, Z. Application of an optical biosensor to study the interaction between porphyrins and wheat germ agglutinin. Wuhan Univ. J. Nat. Sci. 11, 432–436 (2006). https://doi.org/10.1007/BF02832138
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DOI: https://doi.org/10.1007/BF02832138