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Effect of a peptide modeling the nicotinic receptor binding site on the spectral and luminescent properties of dye complexes with cucurbit[8]uril

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Abstract

The paper presents the results of analysis of the effect of a high-affinity peptide (HAP) homologous to a fragment of the nicotinic acetylcholine receptor (nAChR) on the absorption and fluorescence spectra of thiazole orange and thioflavin T complexes with cucurbit[8]uril in aqueous solution. In the presence of HAP, a change in the absorption spectra of the dye complexes and a drop in the fluorescence intensity occur; for thiazole orange, the fluorescence intensity is restored to the initial level in the presence of α-bungarotoxin capable of high-affinity binding to nAChR. The proposed method make it possible to detect the presence of α-bungarotoxin.

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Correspondence to G. V. Zakharova.

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Original Russian Text © G.V. Zakharova, R.R. Konstantinov, A.V. Odinokov, A.K. Chibisov, M.V. Alfimov, I.E. Kasheverov, Yu.N. Utkin, M.N. Zhmak, V.I. Tsetlin, 2016, published in Khimiya Vysokikh Energii, 2016, Vol. 50, No. 2, pp. 127–131.

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Zakharova, G.V., Konstantinov, R.R., Odinokov, A.V. et al. Effect of a peptide modeling the nicotinic receptor binding site on the spectral and luminescent properties of dye complexes with cucurbit[8]uril. High Energy Chem 50, 121–126 (2016). https://doi.org/10.1134/S0018143916020090

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