Publication date: 10th April 2024
Biomaterials are attracting attention because they are inexpensive and environmentally friendly. In recent years, biologically derived materials have been studied for applications not only in the medical field but also in the energy field. It has been suggested that the expression of proton conductivity in proteins is due to the hydration of amino acid peptides. The relationship between hydration and proton conduction of amino acid peptides in proteins is significantly important to elucidate the mechanism of proton conduction in proteins and to apply them to energy devices. In this study, single crystals of glycyl proline (Gly-Pro), which has a cyclic structure and no hydroxyl group on the side chain, and glycyl serine (Gly-Ser), which has no cyclic structure but a hydroxyl group on the side chain, were prepared and the mechanism of proton conductivity in the peptide crystals constituting the protein was investigated from their crystal structures. The crystal structures of these peptide crystals, which are the building blocks of proteins, were used to investigate the mechanism of proton conduction.
Single crystals of the amino acid peptides Gly-Pro and Gly-Ser were prepared and proton conduction and X-ray diffraction measurements revealed that Gly-Pro and Gly-Ser exhibit quasi-one-dimensional and quasi-two-dimensional proton conduction, respectively, depending on the hydration shell bond direction. We also found that Gly-Pro and Gly-Ser crystals exhibit proton conductivity under low hydration conditions due to percolation in which hydration shells in the unit lattice are stochastically interconnected. Furthermore, we have created a new material with high-proton conductivity based on Gly-Ser by genetic recombination.
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