Abstract
We studies the receptor-binding specificity of the synthetic peptide HAP (High Affinity Peptide) and its analogues, which are regarded as a model of the orthosteric site nicotinic acetylcholine receptors (nAChR). Using radioligand analysis, electrophysiology tests, and calcium imaging, we assessed the ability of HAP to interact with nAChR antagonists: long α-neurotoxins and α-conotoxins. A high affinity of HAP for α-bungarotoxin and the absence of its interaction with α-cobratoxin and α-conotoxins was found. The synthesized analogues of HAP in general retained the properties of the original peptide. Thus, HAP cannot be a model of a ligand-binding site.
MeSH terms
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Animals
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Binding Sites
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Bungarotoxins / pharmacology
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Calcium / metabolism
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Cell Line
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Cholinergic Agents / pharmacology*
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Conotoxins / metabolism
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Conotoxins / pharmacology
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Humans
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Membrane Potentials / drug effects
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Membrane Potentials / physiology
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Mice
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Models, Molecular
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Neurotoxins / metabolism
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Neurotoxins / pharmacology
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Oocytes
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Patch-Clamp Techniques
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Peptide Fragments / chemical synthesis
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Peptide Fragments / chemistry
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Peptide Fragments / metabolism*
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Peptide Library
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Radioligand Assay
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Rats
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Receptors, Nicotinic / chemistry
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Receptors, Nicotinic / genetics
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Receptors, Nicotinic / metabolism*
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Torpedo
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Voltage-Sensitive Dye Imaging
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Xenopus laevis
Substances
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Bungarotoxins
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Cholinergic Agents
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Conotoxins
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Neurotoxins
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Peptide Fragments
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Peptide Library
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Receptors, Nicotinic
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Calcium