Year: 2026
Type: preprint
Abstract: Engineering the spatial organization of proteins offers a powerful strategy for controlling biochemical reactions and material properties in synthetic cells. However, dynamically organizing multiple proteins at the nanometer scale remains challenging. We developed asymmetric lipid–oleosin hybrid vesicles in which engineered oleosin molecules served as membrane-forming scaffolds with two orthogonal conjugation systems. External chemical stimuli rapidly recruited two distinct proteins to individual oleosin molecules, generating persistent nanometer-scale proximity, as demonstrated by single-molecule tracking. In an alditol oxidase–horseradish peroxidase cascade, organization of both enzymes on the same oleosin scaffold enhanced product formation compared with intermolecular membrane recruitment. This localized cascade further drove stimulus-responsive polymerization to form membrane-associated cytoskeleton-like structures, increasing vesicle resistance to hypertonic stress. This programmable membrane scaffold couples external signals with molecular organization, enhanced biochemical reactions, and membrane mechanics, providing a framework for engineering synthetic cells that convert chemical inputs into programmable reactions and material outputs.
Source: ChemRxiv
Authors: Masato Suzuki, Rinshi S. Kasai, Koki Kamiya
Institutions: Gunma University, National Cancer Center Research Institute
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: green
Awards: Uncovering the secrets of lipid-transporting ABC proteins, リガンド、会合体、脂質ラフトによる、共同的なWntシグナル生成機構の解明, Measuring molecular properties of membrane proteins using a synthetic cell micro-environment conposed of a model cell membrane and a nanometric space, G503610949, G5336601557, パターン化人工膜とナノ空間を用いた細胞外小胞膜の再構成と膜タンパク質の解析, G7905800975, G8083267976
OpenAlex ID: W7212189057