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. Author manuscript; available in PMC: 2010 Sep 8.
Published in final edited form as: J Am Chem Soc. 2009 Jun 10;131(22):7609–7617. doi: 10.1021/ja8093247

Figure 1.

Figure 1

Figure 1A. Membrane-active peptides from library

Figure 1B. D-amino acid substituted membrane-active peptides

A: The peptides used in this study. These peptides were selected from a 16,384 member combinatorial peptide library using an in vitro high-throughput screen for the ability to permeabilize synthetic lipid vesicles containing 90% phosphatidylcholine lipids and 10% phosphatidylglycerol lipids. Library design, peptide selection and characterization of the active peptides in vitro are described elsewhere8,14,15. The combinatorial sites in the peptides are highlighted in red. The RRG- and –GRR terminal cassettes were also varied combinatorially. On the right side, we give the four letter codes we use herein to represent the peptides. The code is based on the identity of the amino acids in the four combinatorial sites. The asterisk symbols (*) represents the terminal cassettes, when present. B: The D-amino acid substituted peptide homologs used in this study. Four of the peptides above were synthesized with a single D-leucine substitution near the C-terminus to study the coupling of structure to biological activity. The D-leucine is represented by ‘dL’ in blue.