作者: Wu He , Huanjing Dou , Lu Zhang , Lvjing Wang , Ruiyong Wang
DOI: 10.1016/J.SAA.2013.09.027
关键词:
摘要: The interactions between Trypsin and Bicyclol or analogs (Bifendate, I, II III) were investigated by spectrophotometric methods. It was found that had strong ability to quench the intrinsic fluorescence of a static quenching procedure. binding constants obtained at three temperatures. thermodynamics parameters reveal hydrophobic electrostatic play an important role in interaction. Results showed microenvironments tryptophan residue disturbed analogs. indicated Bifendate strongest quencher among five compounds.