Manipulation of a spider peptide toxin alters its affinity for lipid bilayers and potency and selectivity for voltage-gated sodium channel subtype 1.7.
disulfide-rich peptides
drug design
electrophysiology
ion channel
pain
peptide interaction
peptide–lipid membrane
regioselective oxidation
toxin
tri-molecular complex
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
10 04 2020
10 04 2020
Historique:
received:
11
12
2019
revised:
03
03
2020
pubmed:
7
3
2020
medline:
15
12
2020
entrez:
7
3
2020
Statut:
ppublish
Résumé
Huwentoxin-IV (HwTx-IV) is a gating modifier peptide toxin from spiders that has weak affinity for the lipid bilayer. As some gating modifier toxins have affinity for model lipid bilayers, a tripartite relationship among gating modifier toxins, voltage-gated ion channels, and the lipid membrane surrounding the channels has been proposed. We previously designed an HwTx-IV analogue (gHwTx-IV) with reduced negative charge and increased hydrophobic surface profile, which displays increased lipid bilayer affinity and
Identifiants
pubmed: 32139508
pii: S0021-9258(17)48599-1
doi: 10.1074/jbc.RA119.012281
pmc: PMC7152767
doi:
Substances chimiques
Lipid Bilayers
0
NAV1.7 Voltage-Gated Sodium Channel
0
Peptide Fragments
0
Scorpion Venoms
0
Spider Venoms
0
Banques de données
PDB
['5TLR']
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
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