期刊
MOLECULES
卷 17, 期 4, 页码 3945-3956出版社
MDPI
DOI: 10.3390/molecules17043945
关键词
non-covalent modification; superoxide dismutase; hydroxypropyl-beta-cyclo-dextrin; fluorescence intensity; molecular docking
资金
- South-Central University for Nationalities [CZZ10003]
The enzyme activity of superoxide dismutase was improved in the pyrogallol autoxidation system by about 27%, after interaction between hydroxypropyl-beta-cyclodextrin and superoxide dismutase. Fluorescence spectrometry was used to study the interaction between hydroxypropyl-beta-cyclodextrin and superoxide dismutase at different temperatures. By doing this, it can be found that these interactions increase fluorescence sensitivity. In the meantime, the synchronous fluorescence intensity revealed the interaction sites to be close to the tryptophan (Trp) and tyrosine (Tyr) residues of superoxide dismutase. Furthermore, molecular docking was applied to explore the binding mode between the ligands and the receptor. This suggested that HP-beta-CD interacted with the B ring, G ring and the O ring and revealed that the lysine (Lys) residues enter the nanocavity. It was concluded that the HP-beta-CD caused specific conformational changes in SOD by non-covalent modification.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据