Proton Conduction in Gly-X (X = Ser, Ser-Gly-Ser) and GS50.

amino acid biomaterial genetic recombination

Journal

Bioengineering (Basel, Switzerland)
ISSN: 2306-5354
Titre abrégé: Bioengineering (Basel)
Pays: Switzerland
ID NLM: 101676056

Informations de publication

Date de publication:
19 Oct 2023
Historique:
received: 26 08 2023
revised: 09 10 2023
accepted: 12 10 2023
medline: 28 10 2023
pubmed: 28 10 2023
entrez: 28 10 2023
Statut: epublish

Résumé

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

Identifiants

pubmed: 37892953
pii: bioengineering10101223
doi: 10.3390/bioengineering10101223
pmc: PMC10604563
pii:
doi:

Types de publication

Journal Article

Langues

eng

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Auteurs

Hitoki Semizo (H)

Faculty of Science & Engineering, Setsunan University, Ikeda-Nakamachi, Neyagawa 572-8508, Japan.

Ryusei Yabu (R)

Faculty of Science & Engineering, Setsunan University, Ikeda-Nakamachi, Neyagawa 572-8508, Japan.

Yamato Ohgishi (Y)

Faculty of Science & Engineering, Setsunan University, Ikeda-Nakamachi, Neyagawa 572-8508, Japan.

Haruka Kai (H)

Faculty of Science & Engineering, Setsunan University, Ikeda-Nakamachi, Neyagawa 572-8508, Japan.

Hitoshi Nishimura (H)

Faculty of Science & Engineering, Setsunan University, Ikeda-Nakamachi, Neyagawa 572-8508, Japan.

Yasumitsu Matsuo (Y)

Faculty of Science & Engineering, Setsunan University, Ikeda-Nakamachi, Neyagawa 572-8508, Japan.

Classifications MeSH