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Angew Chem Int Ed Engl. 2017 Jul 10;56(29):8495-8499. doi: 10.1002/anie.201703360. Epub 2017 Jun 13.

Δ-Myrtoxin-Mp1a is a Helical Heterodimer from the Venom of the Jack Jumper Ant that has Antimicrobial, Membrane-Disrupting, and Nociceptive Activities.

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Institute for Molecular Bioscience, The University of Queensland, St Lucia, QLD, 4072, Australia.
Medicinal Chemistry, Monash Institute of Pharmaceutical Sciences, Monash University, 381 Royal Parade, Parkville, VIC, 3052, Australia.
Kolling Institute of Medical Research, Royal North Shore Hospital of Sydney, St. Leonards, NSW, 2065, Australia.
Department of Biochemistry and Molecular Biology, Monash University, Wellington Rd, Clayton, Vic, 3800, Australia.


Δ-Myrtoxin-Mp1a (Mp1a), a 49-residue heterodimeric peptide from the venom of Myrmecia pilosula, comprises a 26-mer A chain and a 23-mer B chain 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 4.3 μm. Mp1a also displayed broad-spectrum antimicrobial activity, with the highest potency against Gram-negative Acinetobacter baumannii (MIC 25 nm). Intraplantar injection (10 μm) in mice elicited spontaneous pain and mechanical allodynia. Single- and two-chain mimetics of Mp1a revealed functional selectivity.


antimicrobial peptides; nociceptive pain; peptides; self-assembly; toxins

[Indexed for MEDLINE]

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