In recent years, the use of biomaterials has been required from the viewpoint of biocompatibility of electronic devices. In this study, the proton conductivity of Glycyl-L-serine (Gly-Ser) was investigated to clarify the relationship between hydration and proton conduction in peptides. From the crystal and conductivity data, it was inferred that the proton conductivity in hydrated Gly-Ser crystals is caused by the cleavage and rearrangement of hydrogen bonds between hydration shells formed by hydrogen bonds between amino acids and water molecules. Moreover, a staircase-like change in proton conduction with hydration was observed at n = 0.3 and 0.5. These results indicate that proton transport in Gly-Ser is realized by hydration water. In addition, we also found that hydration of GSGS and GS50 can achieve proton conduction of Gly-Ser tetrameric GSGS and GS50 containing repeating sequences. The proton conductivity at n = 0.3 is due to percolation by the formation of proton-conducting pathways. In addition to these results, we found that proton conductivity at GS50 is realized by the diffusion constant of 3.21 × 10-8 cm2/s at GS50.
Keywords: amino acid; biomaterial; genetic recombination.