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Thermophilic artificial water channels of a lipid-like dendron stabilized by water-containing hydrogen-bonded network
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Thermophilic artificial water channels of a lipid-like dendron stabilized by water-containing hydrogen-bonded network

Chin-Yi Chen, Yuan Chen, Ting-Yen Chang, Mu-Tzu Lee, Shao-Yuan Liu, Ya-Ching Yu, Yu-Hsuan Lin, Cheng-Hsuan Lee, Hsin-Lung Chen, Kuan-Yi Wu, …
Giant, 卷.17, 100220
03/2024

摘要

Amphiphiles Artificial Water Channels Supramolecular chemistry Thermophilic properties Water-induced self-assembly Chemistry (all) Surfaces Coatings and Films Polymers and Plastics Materials Chemistry
Nature modulates the non-covalent interaction of biomolecules to strengthen their structural integrity against various extreme environments. Water, as the key component in living systems, can provide the H-bonded connectivity to readily stabilize the thermophilic proteins toward thermal adaption. However, this brilliant strategy has seldom been utilized in molecular design since the role of water is less explored in synthetic systems. In this study, we design the lipid-like dendron (LD) to form the hydrated hexagonal columnar (Col h ) phase in water-induced self-assembly (WISA). Our findings suggest that the amount of embedded water molecules affects the phase stability of the hydrated Col h phase. The characterization further reveals that remarkable enhancement of phase stability is attributed to the extensive water-containing H-bonded network of the bulk-like core water and interfacial water within the Col h phase. The water-containing H-bonded network prevents artificial water channels (AWCs) in the Col h phase from the destruction of thermal perturbation at temperature higher than the boiling point of water. Moreover, the weakened H-bonded network at high temperatures further accelerates water flow through the AWC of the LD and resulted in the water permeability of an individual AWC (P AWC ) of 1.33 × 10 7 H 2 O·channel −1 ·s −1 at 80 °C. This transporting feature in the weak H-bonded network of the bulk AWCs of the LD is similar to the water transport in the hydrophobic channels such as Aquaporin and other single-molecule AWCs. The study suggests that just like how it does to the thermophilic proteins, water can also use its H-bonded network to enhance the thermal stability of synthetic matter and allow them to perform better functions at higher temperatures.

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https://doi.org/10.1016/j.giant.2023.100220檢視
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