期刊
SPECTROSCOPY LETTERS
卷 50, 期 9, 页码 476-481出版社
TAYLOR & FRANCIS INC
DOI: 10.1080/00387010.2017.1360358
关键词
Bovine hemoglobin; glipizide; molecular docking; spectrometry
类别
资金
- National Science Foundation of China [206275024]
- Hebei Provincial Key Basic Research Program [10967126D]
This study aims to investigate the interaction between glipizide and bovine hemoglobin using fluorescence quenching, circular dichroism spectroscopy in various temperatures (293, 303, and 310K) and molecular docking methods. The results demonstrated that glipizide could cause strong fluorescence quenching of bovine hemoglobin by a dynamic quenching mechanism, during which the hydrophobic interaction played a dominant role in this system. The order of magnitude of binding constant is 10(4), and the number of binding site in the system was close to 1. It also showed that tyrosine residues and tryptophan residues were both involved in the binding of glipizide with bovine hemoglobin, and was closer to the later. Circular dichroism spectra revealed that the conformation of bovine hemoglobin was changed during the binding reaction. The interaction of the system was studied by both spectroscopic method and molecular docking simulation, and the conclusions are consistent.
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