Rational construction of semi-clathrate-like water networks on engineered ferritin cages
7 affiliations
- 1School of Life Science and Technology, Institute of Science Tokyo, Nagatsuta-cho 4259, Midoriku, Yokohama, Japan, 226-8501
- 2Department of Chemistry
- 3Mahindra University, Ecole Centrale School of Engineering
- 4Graduate School of Science
- 5Chiba University
- 6Center of Quantum Life Science for Structural Therapeutics (cQUEST)
- 7Institute of Integrated Research (IIR), Institute of Science Tokyo; Research Center for Autonomous Systems Materialogy (ASMat),, Nagatsuta-cho 4259, Yokohama, Japan, 226-8501
Abstract
Understanding and controlling the organization of water at molecular interfaces is a longstanding goal in both biological and materials sciences, as it controls the biophysical properties of the surfaces. For example, semi-clathrate waters containing polygonal hydrogen-bonded water clusters found in some antifreeze proteins (AFPs), are thought to play key roles in interacting with ice. Despite this significance, the lack of well-defined design principles makes it difficult to rationally construct such ordered hydration architectures. Here, we report the rational construction of a semiclathrate-like water network in an engineered ferritin cage. We designed a series of alanine (Ala) mutants on the internal surface of the ferritin cage and analyzed the formation of semi-clathratelike water networks using X-ray crystal structure analysis. Our results indicate that the continuous hydrophobic surface formed by the Ala mutation organizes water molecules on its surface, forming semi-clathrate-like water networks. Specific hydrogen-bonding networks involving the main-chain carbonyl group were found to play a key role in initiating the formation of semi-clathrate-like water networks. These findings are significant for organizing water molecules on the protein surface to control biophysical properties.
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BibTeX
@misc{maity2026rational,
title = {{Rational construction of semi-clathrate-like water networks on engineered ferritin cages}},
author = {Basudev Maity and Jiaxin Tian and Tadaomi Furuta and Satoshi Yasuda and Takeshi Murata and Takafumi Ueno},
howpublished = {ChemRxiv},
year = {2026},
month = oct,
doi = {10.26434/chemrxiv.15010230/v1},
url = {https://chemrxiv.org/doi/full/10.26434/chemrxiv.15010230/v1},
note = {CC BY},
}
RIS
TY - UNPB
TI - Rational construction of semi-clathrate-like water networks on engineered ferritin cages
AU - Basudev Maity
AU - Jiaxin Tian
AU - Tadaomi Furuta
AU - Satoshi Yasuda
AU - Takeshi Murata
AU - Takafumi Ueno
PY - 2026
DA - 2026/10/11
PB - ChemRxiv
DO - 10.26434/chemrxiv.15010230/v1
UR - https://chemrxiv.org/doi/full/10.26434/chemrxiv.15010230/v1
AB - Understanding and controlling the organization of water at molecular interfaces is a longstanding goal in both biological and materials sciences, as it controls the biophysical properties of the surfaces. For example, semi-clathrate waters containing polygonal hydrogen-bonded water clusters found in some antifreeze proteins (AFPs), are thought to play key roles in interacting with ice. Despite this significance, the lack of well-defined design principles makes it difficult to rationally construct such ordered hydration architectures. Here, we report the rational construction of a semiclathrate-like water network in an engineered ferritin cage. We designed a series of alanine (Ala) mutants on the internal surface of the ferritin cage and analyzed the formation of semi-clathratelike water networks using X-ray crystal structure analysis. Our results indicate that the continuous hydrophobic surface formed by the Ala mutation organizes water molecules on its surface, forming semi-clathrate-like water networks. Specific hydrogen-bonding networks involving the main-chain carbonyl group were found to play a key role in initiating the formation of semi-clathrate-like water networks. These findings are significant for organizing water molecules on the protein surface to control biophysical properties.
ER -