Citation: ZHANG Hong-Yan, ZHOU Ye, WU Ren-An. In-situ Proteomic Characterization of Protein Conformation on Nanoparticle Surface by Cross-linking Mass Spectrometry[J]. Chinese Journal of Analytical Chemistry, ;2018, 46(10): 1570-1580. doi: 10.11895/j.issn.0253-3820.181290
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The conformation change of bovine serum albumin (BSA) absorbed on Fe3O4 nanoparticle surface was characterized by chemical cross-linking mass spectrometry (CXMS)-based proteomics approach. The effects of nanoparticle surface curvatures and initial protein concentrations on protein conformation change were investigated by the CXMS. The results revealed that the BSA adsorbed on the surface of Fe3O4 nanoparticle could undergo an altered conformational state in comparison to that of BSA in solution as the crosslinking frequency of some amino acid residues of the BSA varied significantly, with the assistant analysis of the attenuated total reflectance Fourier transfer infrared spectroscopy (ATR-FTIR). By virtue of the high-throughput, high accuracy and high sensitivity of mass spectrometry, the CXMS-based proteomic method could provide structural information of proteins adsorbed on nanoparticle surface by crosslinking restraints and would be promised to be applied to the analysis of nano-bio interaction for proteins in complex biological systems.
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