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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


Unmasked the influence of amphiphilicity of thiolated ß-peptide nanorods on ordering within monolayers formed on gold surfaces (Chem. Mat. 2007). These studies compared the self-assembly of two sequence isomers. Two-dimensional ordering was shown to be dictated by the ß-peptide sequence, where only a globally amphiphilic ß-peptide formed a well-ordered monolayer; its non-amphiphilic sequence isomer did not.

-Peptide linear sequences (top) and cylinder drawing of folded helices with predicted side-chain volume by a dashed oval (bottom) of globally amphiphilic GA-SH and non-globally amphiphilic isoGA-SH.-Peptide linear sequences (top) and cylinder drawing of folded helices with predicted side-chain volume by a dashed oval (bottom) of globally amphiphilic GA-SH and non-globally amphiphilic isoGA-SH.
β-Peptide linear sequences (left) and cylinder drawing of folded helices with predicted side-chain volume by a dashed oval (right) of globally amphiphilicGA-SH and non-globally amphiphilic isoGA-SH.

Model for organization of β-Peptide SAMs on gold. Left: arrangement globally amphiphilic sequenceGA-SH. Right: non-globally amphiphilic sequence isoGA-SH. Side chains omitted for clarity. Model for organization of β-Peptide SAMs on gold. Left: arrangement globally amphiphilic sequenceGA-SH. Right: non-globally amphiphilic sequence isoGA-SH. Side chains omitted for clarity.
Model for organization of β-Peptide SAMs on gold. Left: arrangement globally amphiphilic sequenceGA-SH. Right: non-globally amphiphilic sequence isoGA-SH. Side chains omitted for clarity.

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