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    The interaction of arginine- and tryptophan-rich cyclic hexapeptides with Escherichia coli membranes

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    Authors
    Junkes, Christof
    Wessolowski, Axel
    Farnaud, Sébastien
    Evans, Robert W.
    Good, Liam
    Bienert, Michael
    Dathe, Margitta
    Affiliation
    Leibniz Institute of Molecular Pharmacology
    Westminster University
    King's College London
    Issue Date
    2008-04
    Subjects
    antimicrobial hexapeptides
    cyclic peptides
    lipopolysaccharides (LPS)
    L-form bacteria
    membrane permeabilization
    outer membrane
    inner membrane
    
    Metadata
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    Abstract
    Cyclization of R- and W-rich hexapeptides has been found to enhance specifically the antimicrobial activity against Gram-negative Escherichia coli. To gain insight into the role of the bacterial outer membrane in mediating selectivity, we assayed the activity of cyclic hexapeptides derived from the parent sequence c-(RRWWRF) against several E. coli strains and Bacillus subtilis, L-form bacteria, and E. coli lipopolysaccharide (LPS) mutant strains, and we also investigated the peptide-induced permeabilization of the outer and inner membrane of E. coli. Wall-deficient L-form bacteria were distinctly less susceptible than the wild type strain. The patterns of peptide-induced permeabilization of the outer and inner E. coli membranes correlated well with the antimicrobial activity, confirming that membrane permeabilization is a detrimental effect of the peptides upon bacteria. Truncation of LPS had no influence on the activity of the cyclic parent peptide, but the highly active c-(RRWFWR), with three adjacent aromatic residues, required the complete LPS for maximal activity. Furthermore, differences in the activity of the parent peptide and its all-D sequence indicated stereospecific interactions with the LPS mutant strains. We suggest that, depending on the primary sequence of the peptides, either hydrophobic interactions with the fatty acid chains of lipid A, or electrostatic interactions disturbing the polar core region and interference with saccharide-saccharide interactions prevail in the barrier-disturbing effect upon the outer membrane and thereby provide peptide accessibility to the inner membrane. The results underline the importance of tryptophan and arginine residues and their relative location for a high antimicrobial effect, and the activity-modulating function of the outer membrane of E. coli. In addition to membrane permeabilization, the data provided evidence for the involvement of other mechanisms in growth inhibition and killing of bacteria.
    Citation
    Junkes, C. et al (2008) 'The interaction of arginine- and tryptophan-rich cyclic hexapeptides with Escherichia coli membranes' J. Pept. Sci. 14 (4):535-43
    Publisher
    Wiley
    Journal
    Journal of peptide science : an official publication of the European Peptide Society
    URI
    http://hdl.handle.net/10547/593506
    DOI
    10.1002/psc.940
    PubMed ID
    17985396
    Additional Links
    http://onlinelibrary.wiley.com/doi/10.1002/psc.940/abstract
    Type
    Article
    Language
    en
    ISSN
    1075-2617
    ae974a485f413a2113503eed53cd6c53
    10.1002/psc.940
    Scopus Count
    Collections
    Cell and Cryobiology Research Group

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