Journal of Hebei University (Natural Science Edition) ›› 2019, Vol. 39 ›› Issue (4): 398-403.DOI: 10.3969/j.issn.1000-1565.2019.04.011

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Screening and identification of sFcγRⅡb binding peptide

XU Zhenzhen1,2, LIU Lipeng1,2, ZHANG Yanfen2,3, CUI Zhe1,2, BI Kewei1,2, LIU Zhongcheng1,2   

  1. 1.College of Pharmaceutical Sciences, Hebei University, Baoding 071002, China; 2.Key Laboratory of Pharmaceutical Quality Control of Hebei Province, Baoding 071002, China; 3.Office of Science and Technology, Hebei University, Baoding 071002, China
  • Received:2018-10-03 Online:2019-07-25 Published:2019-07-25

Abstract: FcγRⅡb is the only inhibitory receptor of the IgG Fc receptor(FcγR)and plays an important role in the negative regulation and immune responses.In order to screen the binding peptide of sFcγRⅡb, the recombinant sFcγRⅡb protein was used as the target molecule, and the sFcγRⅡb binding peptide was screened by phage peptide library display technology.The affinity of each eluted phage to sFcγRⅡb protein was identified by ELISA.40 phage clones were screened after four rounds screening, and 28 different 12-residue peptides were obtained through translation of DNA sequencing data.The affinities between phages and sFcγRⅡb protein were estimated and confirmed by ELISA analysis, and the results showed that the deduced peptide sequence, FHKMPWYMSMYY was the highest specificity and affinity to sFcγRⅡb protein. Furthermore, this study may lay a foundation for the further research on the mechanism of FcγRⅡb and the function of binding peptide.

Key words: sFcγRⅡb, phage display technology, binding peptides

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