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

Authors :
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.
Source :
Angewandte Chemie International Edition. 7/10/2017, Vol. 56 Issue 29, p8495-8499. 5p.
Publication Year :
2017

Abstract

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 μ m. Mp1a also displayed broad-spectrum antimicrobial activity, with the highest potency against Gram-negative Acinetobacter baumannii (MIC 25 n m). Intraplantar injection (10 μ m) in mice elicited spontaneous pain and mechanical allodynia. Single- and two-chain mimetics of Mp1a revealed functional selectivity. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
14337851
Volume :
56
Issue :
29
Database :
Academic Search Index
Journal :
Angewandte Chemie International Edition
Publication Type :
Academic Journal
Accession number :
123928564
Full Text :
https://doi.org/10.1002/anie.201703360