Conductance Switching in Single-Peptide Molecules through Interferer Binding

Li Wen Huang, Yen-Hsun Su, Chao Cheng Kaun

Research output: Contribution to journalArticle

Abstract

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.

Original languageEnglish
Pages (from-to)9191-9195
Number of pages5
JournalACS Omega
Volume3
Issue number8
DOIs
Publication statusPublished - 2018 Aug 31

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Peptides
Molecules
Cysteamine
Metal ions
Copper
Ions
bisphenol A

All Science Journal Classification (ASJC) codes

  • Chemistry(all)
  • Chemical Engineering(all)

Cite this

Huang, Li Wen ; Su, Yen-Hsun ; Kaun, Chao Cheng. / Conductance Switching in Single-Peptide Molecules through Interferer Binding. In: ACS Omega. 2018 ; Vol. 3, No. 8. pp. 9191-9195.
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Conductance Switching in Single-Peptide Molecules through Interferer Binding. / Huang, Li Wen; Su, Yen-Hsun; Kaun, Chao Cheng.

In: ACS Omega, Vol. 3, No. 8, 31.08.2018, p. 9191-9195.

Research output: Contribution to journalArticle

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