Structural requirements and ionic mechanism of the Mytilus inhibitory peptides (MIPs) on Helix central neurons.
1. The structural and ionic requirements for potent FVamide-induced inhibition were investigated using Helix aspersa central neurons under current or voltage clamp. 2. For potent FVamide inhibition the full hexapeptide sequence, GSPYFVamide, was required. The rank order of decreasing potency was GSPYFVamide >> SPYFVamide> PYFVamide > YFVamide. 3. GSPYFVamide inhibition involved an increase in conductance to both potassium and chloride ions as demonstrated by ion substitution experiments and addition of 4-aminopyridine, tetraethylammonium, 4,4-di-isothiocyanatostilbene-2,2'-disulfonic acid, 4,4-dinitrostilbene-2,2'-disulfonic acid disodium salt and furosemide to the solution bathing the preparation.
Pedder
S M
SM
Department of Physiology & Pharmacology, School of Biological Sciences, University of Southampton, UK.
Chen
M L
ML
Muneoka
Y
Y
Walker
R J
RJ
D000818:Animals; D049872:Bivalvia / Q000737:chemistry*; D006372:Helix, Snails; D066298:In Vitro Techniques; D007473:Ion Channels / Q000187:drug effects*; D009474:Neurons / Q000187:drug effects* / Q000378:metabolism; D009842:Oligopeptides / Q000737:chemistry / Q000494:pharmacology*; D010446:Peptide Fragments / Q000494:pharmacology; D013329:Structure-Activity Relationship
D007473:Ion Channels; D009842:Oligopeptides; D010446:Peptide Fragments