Hydrogen bond based smart polymer for highly selective and tunable capture of multiply phosphorylated peptides.

ABSTRACT: Multisite phosphorylation is an important and common mechanism for finely regulating protein functions and subsequent cellular responses. However, this study is largely restricted by the difficulty to capture low-abundance multiply phosphorylated peptides (MPPs) from complex biosamples owing to the limitation of enrichment materials and their interactions with phosphates. Here we show that smart polymer can serve as an ideal platform to resolve this challenge. Driven by specific but tunable hydrogen bonding interactions, the smart polymer displays differential complexation with MPPs, singly phosphorylated and non-modified peptides. Importantly, MPP binding can be modulated conveniently and precisely by solution conditions, resulting in highly controllable MPP adsorption on material surface

SUBMITTER: Qing G 

PROVIDER: S-EPMC5587758 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature