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

Allan M. Torres; Paramjit Bansal; Jennifer M. S. Koh; Guilhem Pagès; Ming J. Wu; Philip W. Kuchel

doi:10.1016/j.febslet.2014.03.044

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

Allan M. Torres, Paramjit Bansal, Jennifer M. S. Koh, Guilhem Pagès, Ming J. Wu, Philip W. Kuchel

School of Science

Research output: Contribution to journal › Article › peer-review

3 Citations (Scopus)

Abstract

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 Î²-defensins, however the presence of a third antiparallel Î²-strand makes its structure more similar to the Î²-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.

Original language	English
Pages (from-to)	1821-1826
Number of pages	6
Journal	FEBS Letters
Volume	588
Issue number	9
DOIs	https://doi.org/10.1016/j.febslet.2014.03.044
Publication status	Published - 2014

Access to Document

10.1016/j.febslet.2014.03.044

Cite this

@article{b5ec2d37b1c44ed3bc404a10e5e60193,

title = "Structure and antimicrobial activity of platypus 'intermediate' defensin-like peptide",

abstract = "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 {\^I}²-defensins, however the presence of a third antiparallel {\^I}²-strand makes its structure more similar to the {\^I}²-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.",

author = "Torres, {Allan M.} and Paramjit Bansal and Koh, {Jennifer M. S.} and Guilhem Pag{\`e}s and Wu, {Ming J.} and Kuchel, {Philip W.}",

year = "2014",

doi = "10.1016/j.febslet.2014.03.044",

language = "English",

volume = "588",

pages = "1821--1826",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "John Wiley and Sons Inc",

number = "9",

}

TY - JOUR

T1 - Structure and antimicrobial activity of platypus 'intermediate' defensin-like peptide

AU - Torres, Allan M.

AU - Bansal, Paramjit

AU - Koh, Jennifer M. S.

AU - Pagès, Guilhem

AU - Wu, Ming J.

AU - Kuchel, Philip W.

PY - 2014

Y1 - 2014

N2 - 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 Î²-defensins, however the presence of a third antiparallel Î²-strand makes its structure more similar to the Î²-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.

AB - 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 Î²-defensins, however the presence of a third antiparallel Î²-strand makes its structure more similar to the Î²-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.

UR - http://handle.uws.edu.au:8081/1959.7/547885

U2 - 10.1016/j.febslet.2014.03.044

DO - 10.1016/j.febslet.2014.03.044

M3 - Article

C2 - 24694388

SN - 0014-5793

VL - 588

SP - 1821

EP - 1826

JO - FEBS Letters

JF - FEBS Letters

IS - 9

ER -

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

Abstract

Access to Document

Other files and links

Fingerprint

Cite this