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Related Concept Videos

Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
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Updated: Jun 12, 2026

Reconstitution of the Bacterial Glutamate Receptor Channel by Encapsulation of a Cell-Free Expression System
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Engineering a Transmembrane Receptor for Coacervate-Based Artificial Cells.

Thijs W van Veldhuisen1, Lou M V Raeven1, Niels van Herwijnen1

  • 1Department of Biomedical Engineering and the Institute for Complex Molecular Systems, Eindhoven University of Technology, Eindhoven 5600 MB, The Netherlands.

Journal of the American Chemical Society
|June 10, 2026
PubMed
Summary
This summary is machine-generated.

Researchers engineered a synthetic transmembrane receptor in artificial cells. This system mimics cell signaling, enabling synthetic signal transduction and bioluminescence upon ligand binding, with potential for diverse applications.

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Area of Science:

  • Biochemistry
  • Synthetic Biology
  • Materials Science

Background:

  • Cell-surface receptors are crucial for cellular communication and response to stimuli.
  • Mimicking membrane-mediated signaling in artificial cells is a growing area of interest for synthetic biology.
  • Artificial cells offer a platform to study and engineer biological processes.

Purpose of the Study:

  • To engineer a modular transmembrane receptor for synthetic signal transduction in artificial cells.
  • To create a system that mimics natural cell-surface receptor function using synthetic components.
  • To demonstrate a method for controlled signal activation and output in a synthetic system.

Main Methods:

  • Engineered a heterodimerizing receptor with coiled-coil interactions and a transmembrane domain.
  • Utilized elastin-like polypeptide (ELP) for membrane insertion and stability in copolymer membranes.
  • Fused receptor subunits to split luciferase domains for bioluminescence-based signal detection.
  • Assembled proteins into copolymer-membrane-decorated coacervates.

Main Results:

  • Successfully inserted engineered proteins into artificial cell membranes, with insertion dependent on ELP sequence.
  • Demonstrated retained protein diffusivity within the synthetic membrane.
  • Achieved dose-dependent receptor activation upon addition of a soluble ditopic ligand.
  • Observed a 5-fold increase in receptor activation, indicated by bioluminescence.

Conclusions:

  • Developed a modular synthetic transmembrane receptor system for signal transduction in artificial cells.
  • The engineered receptor successfully mimics natural cell signaling pathways.
  • This modular platform holds potential for creating diverse synthetic receptors with tunable sensing and output functionalities.