Non-Electroneutrality Generated by Bacteriorhodopsin-Incorporated Membranes Enhances the Conductivity of a Gelatin Memory Device.

We have previously demonstrated the potential of gelatin films as a memory device, offering a novel approach for writing, reading, and erasing through the manipulation of gelatin structure and bound water content. Here, we discovered that incorporating a bacteriorhodopsin (BR)-lipid membrane into the gelatin devices can further increase the electron conductivity of the polypeptide-bound water network and the ON/OFF ratio of the device by two folds. Our photocurrent measurements show that the BR incorporated in the membrane sandwiched in a gelatin device can generate a net proton flow from the counter side to the deposited side of the membrane. This leads to the establishment of non-electroneutrality on the gelatin films adjacent to the BR-incorporated membrane. Our Raman spectroscopy results show that BR proton pumping in the ON state gelatin device increases the bound water presence and promotes polypeptide unwinding compared to devices without BR. These findings suggest that the non-electroneutrality induced by BR proton pumping can increase the extent of polypeptide unwinding within the gelatin matrix, consequently trapping more bound water within the gelatin-bound water network. The resulting rise in hydrogen bonds could expand electron transfer routes, thereby enhancing the electron conductivity of the memory device in the ON state.

Electron transfer through protein-bound water and its bioelectronic application.

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.