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Related Concept Videos

Cholinergic Receptors: Nicotinic01:15

Cholinergic Receptors: Nicotinic

Nicotinic receptors are ligand-gated ion channels that are activated by acetylcholine and nicotine. Upon activation, they cause a rapid increase in the permeability of cells to K+, Na+, and Ca2+, followed by depolarization and excitation. They are in the autonomic ganglia, skeletal neuromuscular junction, CNS, and adrenal medulla.
There are two types of nicotinic receptors: neuromuscular (NM/NM/N1) and neuronal (NN/NN/N2). The two families differ based on their location and selectivity to...
Adrenergic Agonists: Chemistry and Structure-Activity Relationship01:16

Adrenergic Agonists: Chemistry and Structure-Activity Relationship

Adrenergic agonists' structure-activity relationship (SAR) determines their selectivity and efficacy. These agonists comprise a phenylethylamine moiety with an aromatic ring and an ethylamine side chain.
Aromatic ring substitutions: Substituting the aromatic ring with –OH groups at positions 3 and 4 yields catecholamines (e.g., epinephrine), which have a high affinity for adrenoceptors. Hydrogen bonding between –OH groups and receptors enhances adrenergic activity.
Separation of the aromatic...
Cholinergic Antagonists: Chemistry and Structure-Activity Relationship01:29

Cholinergic Antagonists: Chemistry and Structure-Activity Relationship

Cholinergic antagonists bind to cholinergic receptors and limit the effects of acetylcholine and other cholinergic agonists. Based on the specific cholinergic receptor affinity, these antagonists are classified as muscarinic or nicotinic. Anticholinergics interrupt parasympathetic innervations while sympathetic innervations remain uninterrupted. Muscarinic antagonists are also called 'muscarinic antagonists', 'antimuscarinics', or 'parasympatholytics'. Nicotinic antagonists are called...
Direct-Acting Cholinergic Agonists: Chemistry and Structure-Activity Relationship01:22

Direct-Acting Cholinergic Agonists: Chemistry and Structure-Activity Relationship

Cholinergic agonists or cholinomimetics mimic the action of acetylcholine to stimulate the parasympathetic nervous system. They are categorized into direct-acting and indirect-acting agents. The direct-acting cholinergic drugs induce the parasympathetic response by directly binding to the muscarinic or nicotine receptors. In comparison, the indirect-acting cholinergic drugs prevent acetylcholine hydrolysis, indirectly contributing to the extended parasympathetic response.
The direct-acting...
Adrenergic Antagonists: Chemistry and Classification of ɑ-Receptor Blockers01:17

Adrenergic Antagonists: Chemistry and Classification of ɑ-Receptor Blockers

Adrenergic antagonists, or sympatholytics, inhibit adrenoceptor activation driven by catecholamines or agonists. Based on their adrenoceptor specificity, adrenergic blockers can be categorized into two primary groups: α-adrenergic blockers (α-blockers) and β-adrenergic blockers (β-blockers). α-blockers interact with α1 and α2 subtypes of α-adrenoceptors.
Nonselective α-blockers: Nonselective α-blockers contain haloalkylamine or imidazoline moieties. Phenoxybenzamine, with a haloalkylamine...
Adrenergic Receptors: ɑ Subtype01:31

Adrenergic Receptors: ɑ Subtype

Adrenoceptors are classified into α and ꞵ classes based on their potencies to catecholamine agonists. α-adrenoceptors show the following order of catecholamine potency:
Adrenaline ≥ Noradrenaline >> Isoprenaline
α-adrenoceptors are further divided into α1 and α2-adrenoceptors.
α1-Adrenoceptors: These receptors are located postsynaptically on the effector organs and cause constriction of smooth muscle mediated by activation of phospholipase C—inositol-1,4,5-trisphosphate...

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Localization of Plasma Membrane and Intracellular Neuronal Nicotinic Acetylcholine Receptors Using Quantitative Imaging in Mammalian Cells
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Atypical nicotinic agonist bound conformations conferring subtype selectivity.

Motohiro Tomizawa1, David Maltby, Todd T Talley

  • 1Environmental Chemistry and Toxicology Laboratory, Department of Environmental Science, Policy and Management, University of California, Berkeley, CA 94720-3112, USA.

Proceedings of the National Academy of Sciences of the United States of America
|January 31, 2008
PubMed
Summary
This summary is machine-generated.

Investigating nicotinic acetylcholine receptor (nAChR) agonists reveals distinct binding conformations in Lymnaea stagnalis and Aplysia californica AChBPs. This explains neonicotinoid and nicotinoid selectivity between insect and vertebrate nAChRs.

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Local Application of Drugs to Study Nicotinic Acetylcholine Receptor Function in Mouse Brain Slices
10:04

Local Application of Drugs to Study Nicotinic Acetylcholine Receptor Function in Mouse Brain Slices

Published on: October 29, 2012

Area of Science:

  • Neuroscience
  • Pharmacology
  • Structural Biology

Background:

  • Nicotinic acetylcholine receptors (nAChRs) are vital for neurotransmission and are targets for drugs and insecticides.
  • nAChR subtypes exhibit varied sensitivities to different agonists, influencing drug and insecticide efficacy.
  • Acetylcholine-binding proteins (AChBPs) serve as structural surrogates for nAChRs, aiding in the study of agonist interactions.

Purpose of the Study:

  • To investigate the subtype selectivity of nAChR agonists using two distinct AChBPs.
  • To elucidate the structural basis for differential binding of neonicotinoid and nicotinoid agonists.
  • To develop structural models explaining agonist selectivity between insect and vertebrate nAChR subtypes.

Main Methods:

  • Photoaffinity labeling with azido-neonicotinoid and azido-nicotinoid probes.
  • Comparison of probe labeling sites on Lymnaea stagnalis (Ls) AChBP and Aplysia californica (Ac) AChBP.
  • Generation of structural models for Ls-AChBP and Ac-AChBP complexes with agonists.

Main Results:

  • Ls-AChBP was labeled at two distinct sites (loop F Y164 and loop C Y192) by neonicotinoids, and one site (loop C Y192) by nicotinoids.
  • Ac-AChBP was labeled at a single site (loop C Y195/loop E M116) by both neonicotinoid and nicotinoid probes.
  • Structural models revealed distinct bound conformations for neonicotinoids in Ls-AChBP, unlike the conserved conformations in Ac-AChBP.

Conclusions:

  • Subtype selectivity of nAChR agonists is determined by disparate bound conformations, particularly for neonicotinoids in Ls-AChBP.
  • This finding establishes an atypical mechanism for neonicotinoid versus nicotinoid selectivity between insect and vertebrate nAChRs.
  • The study provides critical structural insights into nAChR-agonist interactions, informing future drug and insecticide design.