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Toxins 2015, 7(5), 1683-1701; doi:10.3390/toxins7051683

Natural Compounds Interacting with Nicotinic Acetylcholine Receptors: From Low-Molecular Weight Ones to Peptides and Proteins

1
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow 117997, Russia
2
Institute of Cell Biophysics, Russian Academy of Sciences, Pushchino 142290, Russia
3
Elyakov Pacific Institute of Bioorganic Chemistry, Far East Branch of the Russian Academy of Sciences, Vladivostok 690022, Russia
4
SME Syneuro, Moscow 117997, Russia
These authors contributed equally to this work.
*
Author to whom correspondence should be addressed.
Academic Editor: Bryan Grieg Fry
Received: 28 March 2015 / Accepted: 7 May 2015 / Published: 14 May 2015
(This article belongs to the Special Issue Selected Papers from the 5th Venoms to Drugs Meeting)
View Full-Text   |   Download PDF [811 KB, uploaded 14 May 2015]   |  

Abstract

Nicotinic acetylcholine receptors (nAChRs) fulfill a variety of functions making identification and analysis of nAChR subtypes a challenging task. Traditional instruments for nAChR research are d-tubocurarine, snake venom protein α-bungarotoxin (α-Bgt), and α-conotoxins, neurotoxic peptides from Conus snails. Various new compounds of different structural classes also interacting with nAChRs have been recently identified. Among the low-molecular weight compounds are alkaloids pibocin, varacin and makaluvamines C and G. 6-Bromohypaphorine from the mollusk Hermissenda crassicornis does not bind to Torpedo nAChR but behaves as an agonist on human α7 nAChR. To get more selective α-conotoxins, computer modeling of their complexes with acetylcholine-binding proteins and distinct nAChRs was used. Several novel three-finger neurotoxins targeting nAChRs were described and α-Bgt inhibition of GABA-A receptors was discovered. Information on the mechanisms of nAChR interactions with the three-finger proteins of the Ly6 family was found. Snake venom phospholipases A2 were recently found to inhibit different nAChR subtypes. Blocking of nAChRs in Lymnaea stagnalis neurons was shown for venom C-type lectin-like proteins, appearing to be the largest molecules capable to interact with the receptor. A huge nAChR molecule sensible to conformational rearrangements accommodates diverse binding sites recognizable by structurally very different compounds. View Full-Text
Keywords: α-conotoxins; low-molecular weight agonists and antagonists; α-neurotoxins; nicotinic acetylcholine receptors; snake venom phospholipases A2; three-finger Ly6 proteins α-conotoxins; low-molecular weight agonists and antagonists; α-neurotoxins; nicotinic acetylcholine receptors; snake venom phospholipases A2; three-finger Ly6 proteins
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Kudryavtsev, D.; Shelukhina, I.; Vulfius, C.; Makarieva, T.; Stonik, V.; Zhmak, M.; Ivanov, I.; Kasheverov, I.; Utkin, Y.; Tsetlin, V. Natural Compounds Interacting with Nicotinic Acetylcholine Receptors: From Low-Molecular Weight Ones to Peptides and Proteins. Toxins 2015, 7, 1683-1701.

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