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Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
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Related Experiment Video

Updated: Jan 7, 2026

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy
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Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

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Membrane-Mimetic Micelles Drive Structural Switching in Uperin 3.5.

Sucharita Banerjee1,2,3, Anup Kumar Prasad1,2,3, Lisandra L Martin3

  • 1IITB-Monash Research Academy, Indian Institute of Technology, Bombay 400076, India.

The Journal of Physical Chemistry. B
|January 2, 2026
PubMed
Summary
This summary is machine-generated.

Uperin 3.5, an antimicrobial peptide, shifts between alpha-helical and beta-sheet structures near membranes. This peptide aggregation behavior near zwitterionic micelles offers insights into host-defense peptides and functional amyloids.

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Area of Science:

  • Biochemistry
  • Biophysics
  • Molecular Biology

Background:

  • Uperin 3.5, a peptide from frog skin, exhibits both antimicrobial and amyloidogenic properties.
  • Its conformational flexibility between alpha-helical and beta-sheet structures is key to its physiological roles.
  • Understanding this peptide is crucial for exploring the link between host-defense peptides and functional amyloids.

Purpose of the Study:

  • To investigate the adsorption, conformational changes, and self-assembly of Uperin 3.5 near membrane-mimicking environments.
  • To elucidate the mechanism of Uperin 3.5's structural transitions and aggregation near zwitterionic interfaces.
  • To compare its behavior at zwitterionic versus anionic interfaces for insights into cytotoxicity.

Main Methods:

  • Microsecond-scale molecular dynamics simulations.
  • Utilized dodecylphosphocholine (DPC) micelles to mimic eukaryotic membrane environments.
  • Analyzed peptide adsorption, conformational transitions (alpha-helix to beta-sheet), and self-assembly at the peptide-micelle interface.

Main Results:

  • DPC micelle surface facilitated rapid Uperin 3.5 adsorption and alpha-helix formation (approx. 40% helical content).
  • At higher peptide concentrations (6-7 peptides/micelle), beta-sheet accumulation occurred via self-assembly.
  • A cross-alpha, fibril-like structure with antiparallel beta-sheet dimers as intermediates was observed.
  • Peptides remained surface-associated at zwitterionic DPC micelles, unlike behavior at anionic interfaces.

Conclusions:

  • The peptide-to-surfactant ratio significantly influences Uperin 3.5 aggregation.
  • Uperin 3.5 adopts specific structures near membranes, potentially mitigating cytotoxicity.
  • This study provides a molecular-level understanding of how antimicrobial peptides transition into functional amyloids.