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Bis(zinc(II)-dipicolylamine)-functionalized sub-2 ?m core-shell microspheres for the analysis of N-phosphoproteome.


ABSTRACT: Protein N-phosphorylation plays a critical role in central metabolism and two/multicomponent signaling of prokaryotes. However, the current enrichment methods for O-phosphopeptides are not preferred for N-phosphopeptides due to the intrinsic lability of P-N bond under acidic conditions. Therefore, the effective N-phosphoproteome analysis remains challenging. Herein, bis(zinc(II)-dipicolylamine)-functionalized sub-2??m core-shell silica microspheres (SiO2@DpaZn) are tailored for rapid and effective N-phosphopeptides enrichment. Due to the coordination of phosphate groups to Zn(II), N-phosphopeptides can be effectively captured under neutral conditions. Moreover, the method is successfully applied to an E.coli and HeLa N-phosphoproteome study. These results further broaden the range of methods for the discovery of N-phosphoproteins with significant biological functions.

SUBMITTER: Hu Y 

PROVIDER: S-EPMC7718886 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature

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Bis(zinc(II)-dipicolylamine)-functionalized sub-2 μm core-shell microspheres for the analysis of N-phosphoproteome.

Hu Yechen Y   Jiang Bo B   Weng Yejing Y   Sui Zhigang Z   Zhao Baofeng B   Chen Yuanbo Y   Liu Lukuan L   Wu Qiong Q   Liang Zhen Z   Zhang Lihua L   Zhang Yukui Y  

Nature communications 20201204 1


Protein N-phosphorylation plays a critical role in central metabolism and two/multicomponent signaling of prokaryotes. However, the current enrichment methods for O-phosphopeptides are not preferred for N-phosphopeptides due to the intrinsic lability of P-N bond under acidic conditions. Therefore, the effective N-phosphoproteome analysis remains challenging. Herein, bis(zinc(II)-dipicolylamine)-functionalized sub-2 μm core-shell silica microspheres (SiO<sub>2</sub>@DpaZn) are tailored for rapid  ...[more]

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