Δ-Myrtoxin-Mp1a is a helical heterodimer from the venom of the jack jumper ant that has antimicrobial, membrane-disrupting, and nociceptive activities

Dekan, Zoltan, Headey, Stephen J. , Scanlon, Martin, Baldo, Brian A. , Lee, Tzong-Hsien, Aguilar, Marie-Isabel, Deuis, Jennifer R. , Vetter, Irina, Elliott, Alysha G. , Amado, Maite, Cooper, Matthew A. , Alewood, Dianne and Alewood, Paul F. (2017) Δ-Myrtoxin-Mp1a is a helical heterodimer from the venom of the jack jumper ant that has antimicrobial, membrane-disrupting, and nociceptive activities. Angewandte Chemie, 56 29: 8495-8499. doi:10.1002/anie.201703360


Author Dekan, Zoltan
Headey, Stephen J.
Scanlon, Martin
Baldo, Brian A.
Lee, Tzong-Hsien
Aguilar, Marie-Isabel
Deuis, Jennifer R.
Vetter, Irina
Elliott, Alysha G.
Amado, Maite
Cooper, Matthew A.
Alewood, Dianne
Alewood, Paul F.
Title Δ-Myrtoxin-Mp1a is a helical heterodimer from the venom of the jack jumper ant that has antimicrobial, membrane-disrupting, and nociceptive activities
Journal name Angewandte Chemie   Check publisher's open access policy
ISSN 1521-3773
1433-7851
Publication date 2017-06-13
Sub-type Article (original research)
DOI 10.1002/anie.201703360
Open Access Status Not yet assessed
Volume 56
Issue 29
Start page 8495
End page 8499
Total pages 6
Place of publication Weinheim, Germany
Publisher Wiley - V C H Verlag GmbH & Co. KGaA
Language eng
Formatted abstract
Δ-Myrtoxin-Mp1a (Mp1a), a 49-residue heterodimeric peptide from the venom of Myrmecia pilosula, comprises a 26-mer Achain and a 23-mer Bchain connected by two disulfide bonds in an antiparallel arrangement. Combination of the individual synthetic chains through aerial oxidation remarkably resulted in the self-assembly of Mp1a as a homogenous product without the need for directed disulfide-bond formation. NMR analysis revealed a well-defined, unique structure containing an antiparallel α-helix pair. Dual polarization interferometry (DPI) analysis showed strong interaction with supported lipid bilayers and insertion within the bilayers. Mp1a caused non-specific Ca2+ influx in SH-SY5Y cells with a half maximal effective concentration (EC50) of 4.3μm. Mp1a also displayed broad-spectrum antimicrobial activity, with the highest potency against Gram-negative Acinetobacter baumannii (MIC 25nm). Intraplantar injection (10μm) in mice elicited spontaneous pain and mechanical allodynia. Single- and two-chain mimetics of Mp1a revealed functional selectivity.
Keyword Antimicrobial peptides
Nociceptive pain
Peptides
Self-assembly
Toxins
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: HERDC Pre-Audit
Institute for Molecular Bioscience - Publications
 
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