Conductance Switching in Single-Peptide Molecules through Interferer Binding

Li Wen Huang, Yen Hsun Su, Chao Cheng Kaun

研究成果: Article同行評審

1 引文 斯高帕斯(Scopus)

摘要

Detection of bioprocess-interfering metal ions and molecules is important for healthcare, and peptide single-molecule junctions have shown their potential toward sensing these targets efficiently. Using first-principles calculations, we investigate the conductance of Cys-Gly-Cys and cysteamine-Gly-Gly-Cys peptide junctions, and the effect of its change upon copper-ion (Cu2+) or bisphenol A (BPA) binding. The calculated conductance of the peptides and the Cu2+-peptide complexes agrees well with the experimental data and that of the BPA-bond peptides is further predicted. Our analyses show that the conductance switching mainly comes from the structure deformation of the peptide caused by Cu2+ binding or from the new conduction channel added by BPA binding. Our results suggest that the cysteamine-Gly-Gly-Cys junction can recognize Cu2+ and BPA better than the Cys-Gly-Cys one does.

原文English
頁(從 - 到)9191-9195
頁數5
期刊ACS Omega
3
發行號8
DOIs
出版狀態Published - 2018 八月 31

All Science Journal Classification (ASJC) codes

  • Chemistry(all)
  • Chemical Engineering(all)

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