Journal
ACS APPLIED MATERIALS & INTERFACES
Volume 6, Issue 24, Pages 22743-22750Publisher
AMER CHEMICAL SOC
DOI: 10.1021/am506882b
Keywords
magnetic microspheres; guanidyl; tunable enrichment ability; phosphorylated peptides; mass spectrum
Funding
- State Key Program of National Natural Science of China [21235005]
- National Natural Science Foundation of China [21475044]
- National Natural Science Foundation for Young Scientists of China [21105027]
- Creative Research Group Project, NSFC [2132106]
- National Key Scientific Instrument and Equipment Development Project [2012YQ120044]
- China State Key Basic Research Program Grant [2013CB911202, 2012CB-910601, 2012CB-910101]
- Analytical Method Innovation Program of MOST [2012IM030900]
- Knowledge Innovation program of DICP
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The highly selective and efficient capture of heterogeneous types of phosphopeptides is critical for comprehensive and in-depth phosphoproteome analysis, but it still remains a challenge since the lack of affinity material with large binding capacity and controllable specificity. Here, a new affinity material was prepared to improve the enrichment capacity and endue the tunable specificity by introducing guanidyl onto poly(glycidyl methacrylate) (PGMA) modified Fe3O4 microsphere (denoted as Fe3O4@PGMA-Guanidyl). The thick polymer shell endows the composite microsphere with large amount of guanidyl and is beneficial to enhancing the affinity interaction between phosphopeptides and the material. Interestingly, the Fe3O4@PGMA-Guanidyl possesses tunable enriching ability for global phosphopeptides or only multiphosphopeptides through simple regulation of buffer composition. The composite has large enrichment capacity (200 mg g(-1)), extremely high detection sensitivity (0.5 fmol), high enrichment recovery (91.30%), great specificity, and rapid magnetic separation. Moreover, the result of the application to capture of phosphopeptides from tryptic digest of nonfat milk has demonstrated the great potential of Fe3O4@PGMA-Guanidyl in detection and identification of low-abundance phosphopeptides of interest in biological sample.
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