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

研究成果: Article査読

68 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)13711-13714
ページ数4
ジャーナルJournal of Physical Chemistry B
113
42
DOI
出版ステータスPublished - 2009 10 22

ASJC Scopus subject areas

  • 物理化学および理論化学
  • 表面、皮膜および薄膜
  • 材料化学

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