详细信息

Label-free in-situ monitoring of protein tyrosine nitration in blood by surface-enhanced Raman spectroscopy  ( SCI-EXPANDED收录 EI收录)  

文献类型:期刊文献

英文题名:Label-free in-situ monitoring of protein tyrosine nitration in blood by surface-enhanced Raman spectroscopy

作者:Li, Yuan-Ting;Li, Da-Wei[1];Cao, Yue;Long, Yi-Tao

机构:[1]E China Univ Sci & Technol, Key Lab Adv Mat, Shanghai 200237, Peoples R China; E China Univ Sci & Technol, Dept Chem, Shanghai 200237, Peoples R China

年份:2015

卷号:69

起止页码:1

外文期刊名:BIOSENSORS & BIOELECTRONICS

收录:;EI(收录号:20150800549435);WOS:【SCI-EXPANDED(收录号:WOS:000356642900001)】;

基金:This research was supported by the National Basic Research 973 Program (2013CB733700), National Natural Science Foundation of China (21421004, 21125522, 21327807), the Shanghai Pujiang Program Grant of China (12JC1403500), the Shanghai Municipal Natural Science Foundation, China (14ZR1410800) and the Fundamental Research Funds for the Central Universities (WB1113005).

语种:英文

外文关键词:Protein tyrosine nitration; Label-free in-situ monitoring; Surface-enhanced Raman spectroscopy

摘要:A novel label-free method for the in-situ monitoring of protein tyrosine nitration (PTN) was explored based on surface-enhanced Raman spectroscopy (SERS). Benefiting from the relative weak binding ability of sulfate to silver surface, the Raman signals of nitrated peptides were boosted well with sulfate-aggregated silver nanoparticles (Ag NPs). The distinction of the SERS spectra between non-nitrated peptides and nitrated peptides was obtained by directly comparing SERS bands at 330-400 cm(-1), allowing the rapid identification of PTN. Furthermore, without any pretreatments, the established method was successfully applied in the rapid in-situ dynamic monitoring of the mimic hemin-catalyzed PTN process in synthetic peptide, bovine serum albumin (BSA), and original human blood serum samples. The results indicated that the proposed approach could be a promising in-situ label-free tool for observing PTN process, which may be quite helpful to deeply understand the mechanism of post-translation modification. (C) 2015 Elsevier B.V. All rights reserved.

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