Improving the antibacterial activity and selectivity of an ultra short peptide by hydrophobic and hydrophilic amino acid stretches.

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  • Additional Information
    • Source:
      Publisher: Elsevier Science Ltd Country of Publication: England NLM ID: 9107377 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1464-3405 (Electronic) Linking ISSN: 0960894X NLM ISO Abbreviation: Bioorg Med Chem Lett Subsets: MEDLINE
    • Publication Information:
      Publication: Oxford : Elsevier Science Ltd
      Original Publication: Oxford ; New York : Pergamon Press, c1991-
    • Subject Terms:
      Drug Design*; Amino Acids/*chemistry ; Anti-Bacterial Agents/*chemistry ; Anti-Bacterial Agents/*pharmacology ; Bacteria/*drug effects ; Peptides/*chemistry ; Peptides/*pharmacology ; Salmonella typhi/*drug effects; Amino Acid Sequence ; Microbial Sensitivity Tests ; Microscopy, Electron, Scanning ; Protein Structure, Secondary
    • Abstract:
      The principle of amino acid stretches tagged at the C terminal of Luecrocin I, which is an ultra-short antibacterial peptide, by tryptophan and arginine or lysine has been reported. The choice of amino acid type at each stretch position depends on the hydrophobic and hydrophilic regions visualized in the helical wheel pattern of Luecrocin I. Oligopeptide tagging should also consider the properties such as positive charge, hydrophobicity, the content of hydrophobic amino acids, polar angle, the properly hydrophilic and hydrophobic facets. Amidation at C terminal and lysine substitute for arginine can increase selectivity between mammalian cells (hemolytic and MTT assay) and bacterial cells tested. KT2 and RT2 which have 53% hydrophobic residues, 7 positive charges, 160° polar angle, -0.02 (KT2) and -0.04 (RT2) hydrophobicity were effective against S. typhi DMST 22842, S. epidermidis ATCC 12228, E. coli ATCC 25922 and V. cholerae non-O1, non-O139. The SEM images implied that the antibacterial mechanism of RT2 and KT2 may depend on concentration rather than time. Finally, RT2 and KT2 can be new antibacterial agents or may be further developed for alternative antibiotics.
      (Copyright © 2013 Elsevier Ltd. All rights reserved.)
    • Contributed Indexing:
      Keywords: Helical wheel; Hydrophilic facets; Hydrophobic facets; Luecrocin I; Peptide design
    • Accession Number:
      0 (Amino Acids)
      0 (Anti-Bacterial Agents)
      0 (Peptides)
    • Publication Date:
      Date Created: 20130709 Date Completed: 20140130 Latest Revision: 20130724
    • Publication Date:
      20240829
    • Accession Number:
      10.1016/j.bmcl.2013.06.005
    • Accession Number:
      23831136