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Roles of Amphipathicity and Hydrophobicity in the Micelle-Driven Structural Switch of a 14-mer Peptide Core from a

Héctor Zamora-Carreras1, Beatriz Maestro2, Erik Strandberg3

  • 1Instituto de Química Física Rocasolano (IQFR), Consejo Superior de Investigaciones Científicas (CSIC), Serrano 119, 28006, Madrid, Spain.

Chemistry (Weinheim an Der Bergstrasse, Germany)
|January 26, 2018
PubMed

Insights

Choline-binding repeats (CBRs) undergo a β-hairpin to α-helix transition. Hydrophobicity and amphipathicity are key factors driving this conformational switch in micelle environments.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Microbiology

Background:

  • Choline-binding repeats (CBRs) are common in microbial surface proteins.
  • A specific CBR peptide (LytA239-252) exhibits a unique β-hairpin to α-helix conformational switch in response to detergent micelles.

Purpose of the Study:

  • Investigate the factors governing the β-hairpin to α-helix transition in CBRs.
  • Determine the specific roles of peptide hydrophobicity and helical amphipathicity in this conformational change.

Main Methods:

  • Designed and synthesized variants of the LytA239-252 peptide.
  • Utilized solution NMR, circular dichroism, and fluorescence spectroscopy to study peptide-micelle interactions.
  • Analyzed interactions with dodecylphosphocholine (DPC) micelles.

Main Results:

  • Cross-strand interactions are crucial for β-hairpin stability when turn sequences are suboptimal.
  • Both amphipathicity and hydrophobicity contribute significantly and comparably to helix stabilization in micelles.
  • CBR-derived peptides represent a novel class of peptides interacting with micelles/membranes.

Conclusions:

  • Understanding the structural plasticity of CBRs is vital for comprehending their function in microbial surface proteins.
  • The findings highlight CBRs as a new category of micelle/membrane-interacting peptides with tunable conformational properties.
Keywords:
micellespeptidesprotein foldingprotein structuresstructural biology

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