TiO2 Nanoparticle에 특이적으로 결합하는 Peptide의 Alanine Scanning Mutant의 성질에 관한 연구
Characterization of Alanine Scanning Mutants of a Peptide Specifically Binding to TiO2 Nanoparticles
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초록
본 연구진은 phage display peptide library로부터 TiO2nanoparticle에 binding 하는 peptide를 선별하여 보고한 바있다. 이 중의 하나인 PEP9을 선택하여 alanine scanningmutagenesis를 통하여 mutant peptide를 display하는 phage를 제작하여 TiO2에의 binding을 조사하였다. 그 결과, 4번위치의 proline이 alanine으로 치환된 peptide의 경우binding activity가 10%로 감소하였고, 2번 valine, 3번serine, 5번 isoleucine의 치환 peptide는 binding이 40%로감소하였다. 이러한 사실로 미루어볼 때, PEP9과 TiO2nanoparticle의 결합에는 2, 3, 4, 5번의 아미노산이 만들어내는 3차원적 구조가 중요한 역할을 하는 것으로 결론 내릴수 있었다.
Abstract
We have previously reported the isolation and characterization of peptides binding to TiO2 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 TiO2 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.
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