In:
Angewandte Chemie, Wiley, Vol. 129, No. 29 ( 2017-07-10), p. 8615-8619
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 Ca 2+ influx in SH‐SY5Y cells with a half maximal effective concentration (EC 50 ) 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.
Type of Medium:
Online Resource
ISSN:
0044-8249
,
1521-3757
DOI:
10.1002/ange.v129.29
DOI:
10.1002/ange.201703360
Language:
English
Publisher:
Wiley
Publication Date:
2017
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