Bulletin of the Chemical Society of Japan
Online ISSN : 1348-0634
Print ISSN : 0009-2673
ISSN-L : 0009-2673
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Biofunctional Molecules Inspired by Protein Mimicry and Manipulation
Takahiro Muraoka
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2020 Volume 93 Issue 1 Pages 138-153

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Abstract

This account focuses on synthetic approaches to develop functional molecules on the basis of mimicry and manipulation of proteins. Proteins are one of the central molecules serving vital functions and maintaining biological homeostasis. The sophisticated roles and dynamic functions found in proteins provide lots of useful clues to develop synthetic functional molecules. This account describes the development of synthetic supramolecular ion channels made of multiblock structures that can switch ion transportation in response to external stimuli by mimicking ligand-gated and mechano-responsive transmembrane proteins. Multiblock amphiphiles also perform membrane budding and self-assembly in a bilayer. This account also describes functionalization of poly(ethylene glycol) by structuring, which allows for controlling the thermal properties and protein aggregation suppression. The thermal response of poly(ethylene glycol) is also effective in a solid state to develop crystals showing thermal polymorphic transitions.

This account describes synthetic approaches to develop functional molecules based on the concept to mimic and manipulate proteins. Inspired by the multiblock structures seen in transmembrane proteins, synthetic supramolecular ion channels that respond to ligand and membrane tension are developed. Functionalization of poly(ethylene glycol) by structuring allows for controlling the thermal properties and protein aggregation suppression. Fullsize Image
 
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