Characterization of Alanine Scanning Mutants of a Peptide Specifically Binding to $TiO_{2}$ Nanoparticles

$TiO_{2}$ Nanoparticle에 특이적으로 결합하는 Peptide의 Alanine Scanning Mutant의 성질에 관한 연구

  • Seo, Min-Hee (Departments of Bioscience and Biotechnology Hankuk University of Foreign Studies) ;
  • Chael, Hee-Kwon (Departments of Bioscience and Chemistry Hankuk University of Foreign Studies) ;
  • Myung, Heejoon (Departments of Bioscience and Biotechnology Hankuk University of Foreign Studies)
  • 서민희 (한국외국어대학교 생명공학과) ;
  • 채희권 (한국외국어대학교 화학과) ;
  • 명희준 (한국외국어대학교 생명공학과)
  • Published : 2005.12.01


We have previously reported the isolation and characterization of peptides binding to $TiO_{2}$ nanoparticles from phage display peptide libraries. One of the peptides (PEP9) was selected and mutant peptide-displaying phages were produced by alanine scanning mutagenesis. The mutant phages were subjected to binding analysis to $TiO_{2}$ nanoparticles. When the proline at residue 4 was substituted by alanine, the binding activity was reduced to $10\%$ of that of wild type PEP9. Substitution of valine at residue 2, serine at residue 3, and isoleucine at residue 5 also decreased the binding to $40\%$. Based on these observations, we concluded that the three dimensional structure generated by residues 2-5 was the critical factor for the binding between PEP9 and the nanoparticle.

본 연구진은 phage display peptide library로부터 $TiO_{2}$ nanoparticle에 binding 하는 peptide를 선별하여 보고한바 있다. 이 중의 하나인 PEP9을 선택하여 alanine scanning mutagenesis를 통하여 mutant peptide를 display하는 phage를 제작하여 $TiO_{2}$에의 binding을 조사하였다. 그 결과, 4번 위치의 proline이 alanine으로 치환된 peptide의 경우 binding activity가 $10\%$로 감소하였고, 2번 valine, 3번 serine, 5번 isoleucine의 치환 peptide는 binding이 $40\%$로 감소하였다. 이러한 사실로 미루어볼 때, PEP9과 $TiO_{2}$ nanoparticle의 결합에는 2, 3, 4, 5번의 아미노산이 만들어내는 3차원적 구조가 중요한 역할을 하는 것으로 결론 내릴 수 있었다.



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