Dana A Weinberger

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The rapid emergence of bacterial infections that are resistant to many drugs underscores the need for new therapeutic agents. Here we report that six- and eight-residue cyclic d,l-alpha-peptides act preferentially on Gram-positive and/or Gram-negative bacterial membranes compared to mammalian cells, increase membrane permeability, collapse transmembrane ion(More)
Cyclic peptides with an even number of alternating d,l-alpha-amino acid residues are known to self-assemble into organic nanotubes. Such peptides previously have been shown to be stable upon protease treatment, membrane active, and bactericidal and to exert antimicrobial activity against Staphylococcus aureus and other gram-positive bacteria. The present(More)
Mononuclear, dinuclear, and polymeric Ru(II) complexes formed from terthienylalkylphosphino redox-switchable hemilabile ligands demonstrate that this class of ligand provides electrochemical control over the electronic properties, coordination environments, and reactivities of bound transition metals. Specifically,(More)
Intermodular aminoacyl transfer is the fundamental bond forming reaction in the biosynthesis of polypeptides by ribosomes and nonribosomal peptide synthetases (NRPS).1 Here we report the design and functional characterizations of short R-helical peptides that mimic the aminoacyl loading and intermodular aminoacyl transfer steps of NRPS with aminolysis rate(More)
Ribosomes and nonribosomal peptide synthetases (NRPSs) carry out instructed peptide synthesis through a series of directed intermodular aminoacyl transfer reactions. We recently reported the design of coiled-coil assemblies that could functionally mimic the elementary aminoacyl loading and intermodular aminoacyl transfer steps of NRPSs. These peptides were(More)
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