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Biomolecules
Special Issues
Acetylcholine (Ach) and Acetylcholine Receptors: Textbook Knowledge and New Data
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Acetylcholine (Ach) and Acetylcholine Receptors: Textbook Knowledge and New Data

A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Natural and Bio-inspired Molecules".

Deadline for manuscript submissions: closed (31 May 2021) | Viewed by 2629

Special Issue Editor

Prof. Dr. Victor Tsetlin

E-Mail Website
Guest Editor
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry RAS, Moscow, Russia
Interests: peptide and protein neurotoxins, nicotinic and other Cys-loop receptors
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

This issue will explore the state-of-the-art on acetylcholine and acetylcholine receptors, as important constituents of the cholinergic system. It will include a short history from the discoveries of acetylcholine and nicotinic/muscarinic acetylcholine receptors (nAChRs/ mAChRs) to their cloning and the current knowledge of their spatial structures.

The physiological processes in which acetylcholine and its receptors are involved will be discussed, including signaling cascades following from the metabotropic mAChRs and ligand-gated nAChRs, including those of non-standard metabotropic nAChRs.

Current information on the structure and function of muscle, neuronal, and non-neuronal nAChRs will be presented, including their functions in the nervous and immune systems, as well as information on the diseases (muscle dystrophies, neurodegenerative diseases, channelopathies) associated with their malfunctioning. A special chapter will cover tools, such as peptide and protein neurotoxins, for nAChR analysis.

The advantage of mAChRs is their high-resolution X-ray structures, including those in complexes with agonists/antagonists and with the G proteins, providing information for understanding the mechanisms of action and opening new lines for drug design. For the latter, new data on the intermediate states of both nAChRs and mAChRs and detailed knowledge of the topography of their orthosteric and allosteric sites are important.

Prof. Dr. Victor Tsetlin
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Biomolecules is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • acetylcholine
  • nicotinic acetylcholine receptor
  • muscarinic acetylcholine receptor
  • X-ray analysis
  • cryo-electron microscopy
  • ligand-gated ion channels
  • neuronal and immune systems
  • diseases
  • neurodegenerative diseases
  • channelopathies
  • agonists
  • antagonists
  • neurotoxins

Published Papers (1 paper)

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Research

16 pages, 3420 KiB  
Article
Spatial Structure and Activity of Synthetic Fragments of Lynx1 and of Nicotinic Receptor Loop C Models
by Konstantin S. Mineev, Elena V. Kryukova, Igor E. Kasheverov, Natalia S. Egorova, Maxim N. Zhmak, Igor A. Ivanov, Dmitry A. Senko, Alexey V. Feofanov, Anastasia A. Ignatova, Alexander S. Arseniev, Yuri N. Utkin and Victor I. Tsetlin
Biomolecules 2021, 11(1), 1; https://doi.org/10.3390/biom11010001 - 22 Dec 2020
Cited by 4 | Viewed by 2223
Abstract
Lynx1, membrane-bound protein co-localized with the nicotinic acetylcholine receptors (nAChRs) and regulates their function, is a three-finger protein (TFP) made of three β-structural loops, similarly to snake venom α-neurotoxin TFPs. Since the central loop II of α-neurotoxins is involved in binding to nAChRs, [...] Read more.
Lynx1, membrane-bound protein co-localized with the nicotinic acetylcholine receptors (nAChRs) and regulates their function, is a three-finger protein (TFP) made of three β-structural loops, similarly to snake venom α-neurotoxin TFPs. Since the central loop II of α-neurotoxins is involved in binding to nAChRs, we have recently synthesized the fragments of Lynx1 central loop, including those with the disulfide between Cys residues introduced at N- and C-termini, some of them inhibiting muscle-type nAChR similarly to the whole-size water-soluble Lynx1 (ws-Lynx1). Literature shows that the main fragment interacting with TFPs is the C-loop of both nAChRs and acetylcholine binding proteins (AChBPs) while some ligand-binding capacity is preserved by analogs of this loop, for example, by high-affinity peptide HAP. Here we analyzed the structural organization of these peptide models of ligands and receptors and its role in binding. Thus, fragments of Lynx1 loop II, loop C from the Lymnaea stagnalis AChBP and HAP were synthesized in linear and Cys-cyclized forms and structurally (CD and NMR) and functionally (radioligand assay on Torpedo nAChR) characterized. Connecting the C- and N-termini by disulfide in the ws-Lynx1 fragment stabilized its conformation which became similar to the loop II within the 1H-NMR structure of ws-Lynx1, the activity being higher than for starting linear fragment but lower than for peptide with free cysteines. Introduced disulfides did not considerably change the structure of HAP and of loop C fragments, the former preserving high affinity for α-bungarotoxin, while, surprisingly, no binding was detected with loop C and its analogs. Full article
(This article belongs to the Special Issue Acetylcholine (Ach) and Acetylcholine Receptors: Textbook Knowledge and New Data)
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