Structure and antimicrobial activity of platypus 'intermediate' defensin-like peptide

Torres, Allan M., Bansal, Paramjit, Koh, Jennifer M.S., Pagès, Guilhem, Wu, Ming J., and Kuchel, Philip W. (2014) Structure and antimicrobial activity of platypus 'intermediate' defensin-like peptide. FEBS Letters, 588 (9). pp. 1821-1826.

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The three-dimensional structure of a chemically synthesized peptide that we have called 'intermediate' defensin-like peptide (Int-DLP), from the platypus genome, was determined by nuclear magnetic resonance (NMR) spectroscopy; and its antimicrobial activity was investigated. The overall structural fold of Int-DLP was similar to that of the DLPs and β-defensins, however the presence of a third antiparallel β-strand makes its structure more similar to the β-defensins than the DLPs. Int-DLP displayed potent antimicrobial activity against Staphylococcus aureus and Pseudomonas aeruginosa. The four arginine residues at the N-terminus of Int-DLP did not affect the overall fold, but were important for its antimicrobial potency.

Item ID: 33722
Item Type: Article (Research - C1)
ISSN: 1873-3468
Keywords: β-defensin, defensin like peptide, intermediate-DLP, NMR spectroscopy, platypus, peptide fold
Funders: Australian Research Council (ARC)
Projects and Grants: ARC Discovery Project Grant
Date Deposited: 18 Jun 2014 09:49
FoR Codes: 06 BIOLOGICAL SCIENCES > 0601 Biochemistry and Cell Biology > 060113 Synthetic Biology @ 100%
SEO Codes: 97 EXPANDING KNOWLEDGE > 970106 Expanding Knowledge in the Biological Sciences @ 100%
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