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Studies on the Interaction between Vanillin, Metal Ions and Lysozyme

Author: KongAiRong
Tutor: ZhuSuJuan
School: Yangzhou University
Course: Biochemistry and Molecular Biology
Keywords: Vanillin Metal ion Lysozyme Interaction UV - visible absorption spectrum Fluorescence spectroscopy Circular dichroism Conformation
CLC: Q50
Type: Master's thesis
Year: 2010
Downloads: 105
Quote: 0
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Abstract


The protein is one of the most important biological macromolecules, is a direct expression of biological traits, charged with a variety of physiological functions in vivo. The study of small molecules and proteins at the molecular level interactions and the presence of metal ions such role in many areas of life sciences, chemistry and medicine issues of mutual concern. Therefore, in-depth study of small molecule substances (especially drug small molecules) with the protein's role in the mechanism and the law, not only for clarify life's mysteries, to understand small molecules of great significance in vivo distribution, transport, metabolism, efficacy, and protein structure as and guiding significance for drug design and screening, disease diagnosis. In this paper, spectrometry, respectively, of the small molecule vanillin and interaction of metal ions and lysozyme. The paper includes the following sections: The first section briefly describes the vanillin characteristics, structural and functional properties of lysozyme, and summed up today to study the interaction of small molecules with proteins. The second part of the UV - visible absorption spectroscopy, fluorescence spectroscopy and circular dichroism study of the interaction between vanillin and lysozyme. Fluorescence spectroscopy showed that vanillin have regular quenching the intrinsic fluorescence of lysozyme, and is caused by a complex interaction of static quenching mechanism; quenching constant measured at different temperatures and Table concept of binding constants obtained a vanillin molecule approximately in conjunction with a lysozyme molecule, the force between the main types of hydrogen bonds and van der Waals forces; based on the F x {9864} ster? non-radiative energy transfer theory measured between The combination of distance is 3.01nm. The same time, the conformation of lysozyme by synchronous fluorescence spectroscopy and circular dichroism detection results show that vanillin added lysozyme secondary structure change, and the α-helix content increased trend. Also, examine the impact of vanillin lysozyme enzyme results realized for activation. The third part of the study of the interaction of metal ions with lysozyme. Experimental results show that the metal ions were Lysozyme can characteristic UV absorption peak enhancements and features of the fluorescence quenching. Obtained in accordance with the changes in the fluorescence intensity and fluorescence quenching formula iron ions, copper ions, respectively, with the the lysozyme fluorescence quenching constant, binding constant and the number of binding sites, push obtaining the quenching mechanism is static quenching and determine the thermodynamic parameters the main binding force. The fourth part of the vanillin coexist with the metal ion, lysozyme (such as fluorescence quenching mechanism, the number of binding sites, the force type, enzyme structure change). The experimental results show that, of vanillin with metal ions on the fluorescence of lysozyme has a dual quenching effect, so that the enhanced interaction, and compared with the binary system, the number of binding sites changed.

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