Interaction between 8-methoxypsoralen and trypsin: Monitoring by spectroscopic, chemometrics and molecular docking approaches
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- 作者：Yingying Liu ; Guowen Zhang ; gwzhang@ncu.edu.cn ; Ni Zeng ; Song Hu
- 关键词：Trypsin ; 8-Methoxypsoralen ; Multiple spectroscopy ; MCR&ndash ; ALS method ; Molecular docking
- 刊名：Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy
- 出版年：2017
- 出版时间：15 February 2017
- 年：2017
- 卷：173
- 期：Complete
- 页码：188-195
- 全文大小：1721 K
- 卷排序：173
文摘
The binding of 8-MOP to trypsin was mainly driven by hydrophobic forces. 8-MOP interacted with the catalytic triplet in the active center of trypsin. The binding of 8-MOP to trypsin induced the conformational changes of trypsin. The kinetic process of the interaction was determined by MCR–ALS analysis.