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Title: Diverse Bilayer Morphologies Achieved via α-Helix-to-β-Sheet Transitions in a Short Amphiphilic Peptide

Journal Article · · Langmuir
ORCiD logo [1];  [1];  [1];  [2]
  1. Argonne National Lab. (ANL), Argonne, IL (United States). Center for Nanoscale Materials
  2. Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)

Transmembrane proteins are functional macromolecules that direct the flow of small molecules and ions across a lipid bilayer. Here, we propose the development of helical peptide amphiphiles that will serve as both the bilayer and the functional unit of a self-assembled peptide bilayer membrane. The peptide, K3L12, was designed not only to possess dimensions similar to that of a lipid bilayer but also to yield a structurally robust, alpha-helical bilayer. The formation of alpha-helices is pH-dependent, and upon annealing the sample, a transition from alpha-helices to $$\beta$$-sheets can be controlled, as indicated by optical and vibrational spectroscopies. Imaging the materials confirms morphologies similar to that of a lipid bilayer but rich in $$\alpha$$-helices. Annealing the samples yields a shift in the morphology from bilayers to curled disks, fibers, and sheets. The structural robustness of the material can facilitate the incorporation of many functions into the bilayer assembly.

Research Organization:
Argonne National Laboratory (ANL), Argonne, IL (United States)
Sponsoring Organization:
USDOE Office of Science (SC)
Grant/Contract Number:
AC02-06CH11357
OSTI ID:
1560015
Journal Information:
Langmuir, Vol. 35, Issue 27; ISSN 0743-7463
Publisher:
American Chemical SocietyCopyright Statement
Country of Publication:
United States
Language:
English
Citation Metrics:
Cited by: 4 works
Citation information provided by
Web of Science

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Cited By (3)


Figures / Tables (5)