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Structure and antimicrobial activity of platypus ‘intermediate’ defensin‐like peptide
Author(s) -
Torres Allan M.,
Bansal Paramjit,
Koh Jennifer M.S.,
Pagès Guilhem,
Wu Ming J.,
Kuchel Philip W.
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.03.044
Subject(s) - antimicrobial , peptide , antimicrobial peptides , defensin , beta defensin , chemistry , staphylococcus aureus , antiparallel (mathematics) , pseudomonas aeruginosa , biochemistry , biology , microbiology and biotechnology , bacteria , physics , genetics , quantum mechanics , magnetic field
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.