Antibacterial agents based on the cyclic d,l-α-peptide architecture View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2001-07

AUTHORS

Sara Fernandez-Lopez, Hui-Sun Kim, Ellen C. Choi, Mercedes Delgado, Juan R. Granja, Alisher Khasanov, Karin Kraehenbuehl, Georgina Long, Dana A. Weinberger, Keith M. Wilcoxen, M. Reza Ghadiri

ABSTRACT

The rapid emergence of bacterial infections that are resistant to many drugs underscores the need for new therapeutic agents1,2,3. Here we report that six- and eight-residue cyclic d,l-α-peptides act preferentially on Gram-positive and/or Gram-negative bacterial membranes compared to mammalian cells, increase membrane permeability, collapse transmembrane ion potentials, and cause rapid cell death. The effectiveness of this class of materials as selective antibacterial agents is highlighted by the high efficacy observed against lethal methicillin-resistant Staphylococcus aureus infections in mice. Cyclic d,l-α-peptides are proteolytically stable, easy to synthesize, and can be derived from a potentially vast membrane-active sequence space. The unique abiotic structure of the cyclic peptides and their quick bactericidal action may also contribute to limit temporal acquirement of drug resistant bacteria. The low molecular weight d,l-α-peptides offer an attractive complement to the current arsenal of naturally derived antibiotics, and hold considerable potential in combating a variety of existing and emerging infectious diseases. More... »

PAGES

452-455

References to SciGraph publications

Journal

TITLE

Nature

ISSUE

6845

VOLUME

412

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/35086601

    DOI

    http://dx.doi.org/10.1038/35086601

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1006592221

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/11473322


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