作者: Wen-Rui Wang , Rong-Rong Zhu , Rong Xiao , Hui Liu , Shi-Long Wang
DOI: 10.1007/S12011-010-8823-X
关键词: Protein structure 、 Circular dichroism 、 Chromatography 、 Chemistry 、 Fluorescence spectrometry 、 Trypsin 、 Enzyme assay 、 Binding constant 、 Fluorescence 、 Protein secondary structure
摘要: In this work, the interaction between nano-TiO2 and trypsin was investigated, mechanisms of were explored by methods UV–vis detection, circular dichroism (CD), fluorescence. The results clearly demonstrated that had an inhibitory effect on enzyme activity. activity decreased to 64% untreated in presence 300 μg/ml nano-TiO2. UV spectrometry proved a strong physical absorption trypsin, CD spectra revealed secondary structure partly destroyed while bound together with ratio α-helix increased from 7.9% 12.8% 100 TiO2 β-sheet 48.7% 36.4%. Furthermore, fluorescence indicated could quench intrinsic through static quenching. Meanwhile, binding constant calculated be 1, process spontaneous molecular procedure which electrostatic plays major role. Our study provide useful approach for evaluating health risk nanomaterials level proteins.