Wormlike micelle formation in peptide-lipid conjugates driven by secondary structure transformation of the headgroups

Tomoko Shimada, Sangwoo Lee, Frank S. Bates, Atsushi Hotta, Matthew Tirrell

Research output: Contribution to journalArticle

65 Citations (Scopus)

Abstract

Wormlike micelles are assemblies of amphiphilic molecules of intermediate mean curvature between spherical micelles and flat bilayer membranes, which often form in solutions of peptide amphiphiles (hydrophilic peptide modules conjugated to hydrophobic subunits). In an effort to better understand the factors controlling peptide amphiphile (PA) micellar shape, we synthetically linked a short peptide with an a-helix-forming tendency to a hexadecyl tail. These molecules initially dissolve as spherical micelles, which can persist for hours or days, followed by transformation to wormlike micelles, which occurs simultaneously with a transition in the secondary structure of the headgroup peptides to β-sheet. This observation provides evidence that the extended micelle is the thermodynamically favored state sought by PA micelles in the process of forming β-sheet structures among the head-groups, though they are not the structures formed during the initial kinetics of assembly.

Original languageEnglish
Pages (from-to)13711-13714
Number of pages4
JournalJournal of Physical Chemistry B
Volume113
Issue number42
DOIs
Publication statusPublished - 2009 Oct 22

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Surfaces, Coatings and Films
  • Materials Chemistry

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