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Analysis of binding centers in nicotinic receptors with the aid of synthetic peptides.
Kasheverov IE
,
Kryukova EV
,
Kudryavtsev DS
,
Ivanov IA
,
Egorova NV
,
Zhmak MN
,
Spirova EN
,
Shelukhina IV
,
Odinokov AV
,
Alfimov MV
,
Tsetlin VI
.
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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.
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