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• W2940084304 abstract "This article reports that a metastructure of polypeptides with the bound water can have high and stable electron conductivity without classic electron-conducting components. We used gelatin as the model protein since the peptide chains contain numerous sites capable of forming hydrogen bonds with water molecules. The lack of redox sites and the trace amounts of aromatic amino acids also eliminate the possibility that the electron transfer is due to redox reactions or pi-stacking. Our Raman spectroscopy results show that the high electron-conductive metastructure is composed of bound water and unwound gelatin polypeptides. Further removal of bound water from the metastructure dramatically decreases the electron-conductivity, indicating that bound water is crucial to connect the polypeptide chains for the electron-conductivity. In addition, the ability to switch between the low-electron-conductive typical hydrogel state and the high-electron-conductive metastructure state of the gelatin hydrogel allows the gelatin hydrogel to exhibit rewritable nonvolatile resistive memory features. The high ON/OFF current ratio of 105 at a low reading voltage of 0.09 V is superior to that of conventional nonvolatile resistive memories by one order of magnitude. The discovered phenomenon of using bound water and flexible polypeptide structure for long-distance electron transfer could provide a new direction for designing highly biocompatible conducting materials or functional devices in bioelectronics." @default.
• W2940084304 created "2019-04-25" @default.
• W2940084304 creator A5001917186 @default.
• W2940084304 creator A5031911658 @default.
• W2940084304 date "2019-07-01" @default.
• W2940084304 modified "2023-10-16" @default.
• W2940084304 title "Electron transfer through protein-bound water and its bioelectronic application" @default.
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• W2940084304 doi "https://doi.org/10.1016/j.bios.2019.04.012" @default.
• W2940084304 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/31029005" @default.
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