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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


Exploited sequence control of ß-peptides to identify a family of non-globally amphiphilic molecules that form lyotropic liquid crystals (Angew. Chemie Int. Ed, 2008). 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). Experiments demonstrated that sequence control provides a general approach to manipulation of the self-assembly of the ß-peptides. It was also shown that the collective properties of these systems are exquisitely sensitive to subtle variations in the nanoscopic patterning of chemical functionality on the ß-peptides (JACS, 2006).

β-Peptide sequences (top) and cylinder representations (bottom) of globally amphiphilic iso-A and non-globally amphiphilic A.
β-Peptide sequences (top) and cylinder representations (bottom)
of globally amphiphilic iso-A and non-globally amphiphilic A.
Optical micrographs of solutions of -Peptides between crossed polarizing filters. A) iso-A (10wt%), B) A (10wt%).
Optical micrographs of solutions of -Peptides between crossed polarizing filters. A) iso-A (10wt%), B) A (10wt%).
Optical micrographs of solutions of β-Peptides between crossed polarizing filters. A) iso-A (10wt%), B) A (10wt%).

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