An international joint research group including Professor Takeshi Fukuma and Project Assistant Professor Ayhan Yurtsever at Nano Life Science Institute, Kanazawa University, Program-Specific Senior Lecturer Takashi Sumikama at the Graduate School of Biostudies, Kyoto University, and Professor Mehmet Sarikaya at the University of Washington succeeded for the first time in the world in directly visualizing that water molecules surrounding protein surfaces form highly ordered 3D structures depending on amino acid sequences. The findings were published in Nature Communications.
Yurtsever A., et al., Nat Commun (2026)
Directly observing what 3D structures water molecules around proteins form at molecular levels served as a major issue over many years. Using peptide systems self-assembling regularly as model samples, the research group conducted high-resolution 3D-AFM observations.
As a result, they clarified that water molecules in vicinities of peptide surfaces are ordered across multiple layers, and that their arrangement modes are determined by amino acid sequences and surface chemical characteristics.
Formed hydration structures were maintained across multiple layers until converging into bulk water, functioning as hydration fingerprints reflecting chemical features of surfaces. These results indicate possibilities that in understanding protein functions, hydration structures exist as a third important information layer, in addition to amino acid sequences and 3D structures emphasized conventionally.
Defining whole proteins including these hydration structures as protein superstructures, the research group proposed a new framework for understanding function expression of biomolecules.
In the future, expanding targets to more complex proteins and biological systems, they aim at constructing new protein function prediction models incorporating hydration structures. Expansions to diverse fields are expected, such as target molecule design in drug discovery, protein engineering, protein design via AI, biosensors, catalytic interface design, and biomimetic material development.
Journal Information
Publication: Nature Communications
Title: Peptides display multilayered hydration shell substructures dictated by sequence-specific surface chemistry
DOI: 10.1038/s41467-026-76923-4
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