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

Bis(zinc(II)-dipicolylamine)-functionalized sub-2 μm core-shell microspheres for the analysis of N-phosphoproteome.
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DOI:
10.1038/s41467-020-20026-1
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发表时间:
2020-12-04
影响因子:
16.6
通讯作者:
Zhang Y
Zhang Y
中科院分区:
综合性期刊1区
文献类型:
--
作者:
Hu Y;Jiang B;Weng Y;Sui Z;Zhao B;Chen Y;Liu L;Wu Q;Liang Z;Zhang L;Zhang Y

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蛋白质 N-磷酸化在原核生物的中央代谢和双/多组分信号传导中起着至关重要的作用。然而,由于 P-N 键在酸性条件下固有的不稳定性,目前 O-磷酸肽的富集方法对于 N-磷酸肽来说并不优选。因此,有效的 N-磷酸蛋白质组分析仍然具有挑战性。在此,双(锌(II)-二吡啶胺)功能化的亚2μm核壳二氧化硅微球(SiO2@DpaZn)专为快速有效地富集N-磷酸肽而设计。由于磷酸基团与Zn(II)的配位,N-磷酸肽可以在中性条件下被有效捕获。此外,该方法还成功应用于大肠杆菌和 HeLa N-磷酸蛋白质组研究。这些结果进一步拓宽了发现具有重要生物学功能的N-磷蛋白的方法范围。 N-磷酸化在中枢代谢和信号传导过程中起着至关重要的作用,然而,N-磷酸肽的富集方法受到P-N键不稳定性的限制。在这里,作者报道了双(锌(II)-二吡啶二胺)功能化的二氧化硅微球的合成和在 N-磷酸肽有效富集中的用途。
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 (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. N-phosphorylation plays a critical role in central metabolism and signaling processes, however, enrichment methods for N-phosphopeptides are limited by the P-N bond lability. Here, the authors report the synthesis and use of silica microspheres functionalized with bis(zinc(II)-dipicolylamine) in N-phosphopeptides effective enrichment.
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