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UW-Madison

  Abbott Research Group - UW Chemical and Biological Engineering

Laboratory for Molecular Engineering
Department of Chemical and Biological Engineering

Self-Assembly of Non-Natural Peptides


Inspired by nature’s use of α-amino acid-based proteins to perform a range of functions, our laboratory has recently initiated a line of investigation that seeks to design organic materials (including lyotropic liquid crystals) using non-natural ß-amino acid oligomers and polymers ("ß-peptides”). This research, pursued through collaboration with organic chemist Sam Gellman at University of Wisconsin, takes advantage of the high stability of the secondary structure of ß-peptides (relative to α-peptides) to create molecules in which functional side chains (displayed in unique order along the molecule) are precisely presented in three-dimensional space. Helical ß-peptides engineered to possess properties of rigid rods with unique patterns of surface functionality have been exploited to design lyotropic liquid crystals using non-globally amphiphilic molecules as well as to create functional organic interfaces. Highlights of this research include:

  • Exploited sequence control of ß-peptides to identify a family of non-globally amphiphilic molecules that form lyotropic liquid crystals This finding is noteworthy because very few non-globally amphiphilic molecules are known to form lyotropic liquid crystals (in contrast, many amphiphilic molecules (surfactants) form liquid crystals). more
  • Revealed sequence-specific assembly of ß-peptide oligomers into hollow nanotubes by using small angle x-ray scattering. more
  • Unmasked the influence of amphiphilicity of thiolated ß-peptide nanorods on ordering within monolayers formed on gold surfaces. These studies compared the self-assembly of two sequence isomers. more