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Mangosteen flavonoids and metal ions , serum albumin and DNA interaction studies

Author: ZhangYuLi
Tutor: WeiYongFeng
School: Northwestern University
Course: Analytical Chemistry
Keywords: α-mangostin β-mangostin metal ions UV-Vis spectra fluorescence spectra serum albumin DNA
CLC: Q523
Type: Master's thesis
Year: 2009
Downloads: 201
Quote: 0
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Abstract


Mangostins have antibacterial, anti-inflammatory, antioxidant, antitumor biological and pharmacological activities, and also can inhibit HIV virus. Due to these biological and pharmacological activities, mangostins were paid much more attention in recent years. Our research focused on the interactions between mangostins and metal ions, serum albumins and DNA. The main contents and conclusions are as following:Firstly, Compared to the UV-Vis spectra of a-mangostin （α-MAG） andγ-mangostin （γ-MAG）, the variation of UV-vis spectra of the complexes of theα-MAG andγ-MAG with metal ions, including Mg2+, Al3+ and Fe3+ et al, was investigated by UV-Vis spectrometry. Through measurement of the UV-Vis absorbance of the reaction solution containing different concentrations of the two MAGs and metal ions, the stoichiometric compositions of the complexes were determined according to the molar ratio method. Meanwhile the molar absorptivity and stablity constant of the complex were derived further. The results show that there are obvious changes in the UV-Vis spectra before and after the complexes of the two MAGs with metal ions formed. After the formation of the complexes of the two MAGs with metal ions, there occurs a bathchromic shift of the maximum absorption wavelength for the two MAGs, which may contribute to the coordination role of the hydroxyl group and keto group of the two MAGs. The stoichiometric compositions （[M]/[L]） of the complexes formed betweenα-MAG and Al3+, Fe3+ are 1: 1 and 1: 2, respectively. The stablity constants are 2.857×106 and 1.527×109, correspondingly. The stoichiometric compositions （[M]/[L]） of the complexes formed betweenγ-MAG and Mg2+, Al3+, Fe3+ and Cu2+ are 1: 2, 1: 1, 1: 1 and 1: 2, respectively. The stablity constants are 1.200×109、2.227×106、2.251×106 and 2.311×109, correspondingly. Secondly, The interaction betweenα-MAG and bovine serum albumin （BSA） or human serum albumin （HSA） was studied by fluorescence spectrometry. The results indicate that the mechanism of the quenching betweenα-MAG and BSA is a dynamic quenching process. The binding constants at 289K and at 300K are calculated to be 1.309×105 and 6.776×104 respectively, and the number of binding sites is about one. The binding locality is a distance 1.70 nm away from tryptophan residue based on Forster non-radiation energy transfer mechanism. The binding power is mainly the hydrogen bond and van der Waals force according to the thermodynamic parameters, the mechanism of the quenching betweenα-MAG and HSA is a dynamic quenching process. The binding constants at 298K and at 308K are calculated to be 3.327×104 and 1.349×104 respectively, and the number of binding sites is about one. The binding locality is a distance 1.82 nm away from tryptophan residue based on Forster non-radiation energy transfer mechanism. The binding power is mainly the hydrophobic force according to the thermodynamic parameters. Thirdly, The interactions betweenγ-MAG and deoxyribonucleic acid （DNA） were investigated in Tris-HCl buffer （pH=7.4） by fluorescence spectrometry and UV-vis absorption spectrometry, and were verified through viscosity method. The results indicate that DNA can obviously increase the fluorescence intensity ofγ-MAG, the part intercalative binding is the major model forγ-MAG and DNA, the ionic strength has an obvious effect on the interaction betweenγ-MAG and DNA.

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CLC: > Biological Sciences > Biochemistry > Nucleic acid > Deoxyribonucleic acid (DNA)
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