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- Title
Proton Conduction in Gly-X (X = Ser, Ser-Gly-Ser) and GS50.
- Authors
Semizo, Hitoki; Yabu, Ryusei; Ohgishi, Yamato; Kai, Haruka; Nishimura, Hitoshi; Matsuo, Yasumitsu
- Abstract
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.
- Subjects
PROTON conductivity; WATER of crystallization; HYDROGEN bonding; PROTONS; AMINO acids; ELECTRONIC equipment; GENETIC recombination; PROTON transfer reactions
- Publication
Bioengineering (Basel), 2023, Vol 10, Issue 10, p1223
- ISSN
2306-5354
- Publication type
Article
- DOI
10.3390/bioengineering10101223