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Peptide-based Identification of Functional Motifs and their Binding Partners
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SNARE Modulators and SNARE Mimetic Peptides.

Mikhail Khvotchev1, Mikhail Soloviev2

  • 1Department of Biochemistry, Center for Neuroscience, Faculty of Science, Mahidol University, Bangkok 10400, Thailand.

Biomolecules
|December 23, 2022
PubMed
Summary
This summary is machine-generated.

Functional peptides are being developed to control soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptor (SNARE) protein activity in membrane trafficking. These SNARE-mimetic systems offer new ways to engineer biological membrane fusion and protein complex assembly.

Keywords:
SNARE mimeticSNARE motifSNARE peptideSNARE proteinSNAREpinsclostridial neurotoxinsfunctional peptidefusogenmembrane fusionmolecular self-assembly

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein (SNAP) receptor (SNARE) proteins are crucial for intracellular membrane trafficking.
  • SNARE proteins facilitate the movement of membranes and cargo between cellular compartments and the extracellular environment.
  • These proteins possess a simple structure with distinct domains, including the SNARE motif, that mediate interactions.

Purpose of the Study:

  • To review recent advancements in designing functional peptides that modulate SNARE protein interactions and functions.
  • To explore the development of SNARE-mimetic systems for applications in membrane fusion and supramolecular complex formation.
  • To discuss the exploitation of SNARE motif self-assembly for engineered polypeptide assembly.

Main Methods:

  • Review of literature on functional peptides targeting SNARE-binding interfaces.
  • Evaluation of SNARE-mimetic systems based on peptide-nucleic acids (PNAs) and coiled coil peptides.
  • Analysis of self-assembly properties of SNARE motifs for polypeptide engineering.

Main Results:

  • Development of functional peptides capable of modifying SNARE-binding interfaces.
  • Demonstration of SNARE-mimetic systems for biological membrane fusion.
  • Creation of large supramolecular protein complexes using peptide-based strategies.
  • Exploitation of SNARE motif self-assembly for on-demand polypeptide assembly.

Conclusions:

  • Functional peptides offer a promising avenue for controlling SNARE-mediated membrane trafficking.
  • SNARE-mimetic systems, including PNA and coiled coil peptides, show potential for engineering membrane fusion and protein assemblies.
  • The self-assembly capacity of SNARE motifs can be leveraged for advanced polypeptide construction and complex re-engineering.