Screening of peptide sequences with affinity to bisphenol a by biopanning

Ik Keun Yoo, Woo Seok Choe

Research output: Contribution to journalArticlepeer-review

5 Scopus citations

Abstract

Bisphenol A (BPA) is a highly hazardous component to human since it is regarded as one of endocrine disruptors. For the analysis and/or removal of BPA, the searching for the specific ligand with a selective affinity to target BPA is required. In order to find the peptide moiety that specifically binds to BPA, the ultrasound-assisted biopanning was carried out with a phage-displayed peptide library expressing constrained heptamer. After six rounds of positive screening against BPA particles followed by the negative screening against the surface of eppendorf tube, the peptide sequence (CysLysSerLeuGluAsnSerTyrCys) with affinity to BPA was screened based on the order of frequency from the screened phage clones. To further verify the specificity of screened peptide sequence, the cross-binding affinity of the phage peptide toward BPA analogues such as Bisphenol S (BPS) and Bisphenol F (BPF) was also assessed, where the selected phage peptide showed a higher affinity to BPA over BPS and BPF.

Original languageEnglish
Pages (from-to)211-214
Number of pages4
JournalKorean Journal of Microbiology
Volume49
Issue number2
DOIs
StatePublished - 2013

Keywords

  • Biopanning
  • Bisphenol A
  • Endocrine disruptor
  • Peptide
  • Ultrasound

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