Study on the structural changes of bovine serum albumin with effects on polydatin binding by a multitechnique approach |
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| Authors: | Peng Xialian Yao Di Pan Yingming Yu Qing Ni Shouhai Bian Hedong Huang Fuping Liang Hong |
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| Affiliation: | Key Laboratory for the Chemistry and Molecular Engineering of Medicinal Resources (Ministry of Education of China), School of Chemistry & Chemical Engineering of Guangxi Normal University, Guilin 541004, PR China. |
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| Abstract: | Polydatin is a traditional Chinese medicine which shows effective biological activity as antimicrobial and antiviral agent. The secondary structure changes of bovine serum albumin (BSA) were investigated by the methods of Fourier transform infrared spectroscopy (FT-IR), circular dichroism (CD) and Raman spectroscopy. The experimental results indicated that polydatin changed the secondary structure of BSA. The presence of polydatin decreased α-helix content of BSA. The conformations of disulfide bridges and the microenvironment of Tyr, Trp residues were also changed. |
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