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Updated: May 16, 2025

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SAAP-148 Oligomerizes into a Hexamer Forming a Hydrophobic Inner Core.

Aden Hodzic1, Djenana Vejzovic2, Altea Topciu2

  • 1NanoEntum, Ruckerlbergergürtel 10, 8010, Graz, Austria.

Chembiochem : a European Journal of Chemical Biology
|April 1, 2025
PubMed
Summary
This summary is machine-generated.

The antimicrobial peptide SAAP-148 forms a stable hexameric structure, crucial for its potent activity against multidrug-resistant bacteria. This structure facilitates membrane interaction and bacterial eradication without inducing resistance.

Keywords:
lipid–peptide interactionsSAAP‐148antimicrobial peptideshydrophobic corespeptide aggregates

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Area of Science:

  • Antimicrobial Peptides
  • Structural Biology
  • Drug Discovery

Background:

  • Human cathelicidin LL-37 derivatives, like SAAP-148, show potent in vitro activity against multidrug-resistant bacteria.
  • SAAP-148's amphipathic nature and cationic charge are key to its membrane interaction and bactericidal mechanism.
  • The secondary and quaternary structures of SAAP-148 and their role in its function remain underexplored.

Purpose of the Study:

  • To elucidate the secondary and quaternary structures of SAAP-148.
  • To investigate how SAAP-148's structure contributes to its antimicrobial activity.
  • To understand the peptide's behavior at the membrane interface.

Main Methods:

  • Circular dichroism (CD) spectroscopy
  • Nuclear Magnetic Resonance (NMR) spectroscopy
  • X-ray scattering
  • AlphaFold 3 protein folding software
  • Molecular dynamics (MD) simulations

Main Results:

  • SAAP-148 forms a stable hexameric bundle comprising three parallel dimers with a hydrophobic core.
  • This hexameric structure is maintained at the membrane interface.
  • MD simulations revealed the formation of fiber-like structures on anionic membranes, stabilized by aromatic residues.

Conclusions:

  • SAAP-148's stable hexameric structure is critical for its potent antimicrobial efficacy.
  • The peptide's quaternary structure facilitates interaction with bacterial membranes, leading to bacterial eradication.
  • The structural insights provide a basis for developing novel antimicrobial agents targeting resistant bacteria.