Results 11 to 20 of about 917,242 (94)

α-Conotoxin [S9A]TxID Potently Discriminates between α3β4 and α6/α3β4 Nicotinic Acetylcholine Receptors [PDF]

open access: yesJournal of Medicinal Chemistry, 2017
α3β4 nAChRs have been implicated in various pathophysiological conditions. However, the expression profile of α3β4 nAChRs and α6/α3β4 nAChRs overlap in a variety of tissues.
Dongting Zhangsun   +2 more
exaly   +3 more sources

Head-to-Tail Cyclization of α-Conotoxin TxID Leads to Enhanced Stability in Serum

open access: yes, 2023
<p>Peptide biomolecules have important bioactivities and hence their use in drug design and development studies has increased in recent years. Conotoxins are natural peptides that obtained from cone snail venoms and have the potential to be used ...
Muharrem AKCAN   +3 more
core   +1 more source

AChBP-targeted alpha-conotoxin correlates distinct binding orientations with nAChR subtype selectivity [PDF]

open access: yes, 2007
Neuronal nAChRs are a diverse family of pentameric ion channels with wide distribution throughout cells of the nervous and immune systems. However, the role of specific subtypes in normal and pathological states remains poorly understood due to the lack ...
Sixma, Titia K.   +46 more
core   +1 more source

Solution structure of α-conotoxin SI [PDF]

open access: yes, 2000
The nuclear magnetic resonance solution structure of α-conotoxin SI has been determined at pH 4.2. The 36 lowest energy structures show that α-conotoxin SI exists in a single major solution conformation and is stabilized by six hydrogen bonds ...
Hargittai, Balazs   +9 more
core   +1 more source

Ion Channels as Marine Drug Targets [PDF]

open access: yes, 2020
Marine Drugs is glad to announce its first Special Issue book on “ion channels” related research: Under the great stewardship of the Guest Editor, Dr.

core   +2 more sources

Solution Structure and Acid-Base Properties of Reduced α-Conotoxin MI [PDF]

open access: yes, 2021
The reduced derivative of α-conotoxin MI, a 14 amino acid peptide is characterized by NMR-pH titrations and molecular dynamics simulations to determine the protonation constants of the nine basic moieties, including four cysteine thiolates, and the ...
Pálla, Tamás   +13 more
core   +1 more source

Structural mechanisms for α-conotoxin activity at the human α3β4 nicotinic acetylcholine receptor

open access: yes, 2017
Nicotinic acetylcholine receptors (nAChR) are therapeutic targets for a range of human diseases. α-Conotoxins are naturally occurring peptide antagonists of nAChRs that have been used as pharmacological probes and investigated as drug leads for nAChR ...
Paul F. Alewood   +5 more
core   +2 more sources

α-Conotoxin Peptidomimetics:Probing the Minimal Binding Motif for Effective Analgesia [PDF]

open access: yes, 2020
Several analgesic α-conotoxins have been isolated from marine cone snails. Structural modification of native peptides has provided potent and selective analogues for two of its known biological targets-nicotinic acetylcholine and γ-aminobutyric acid ...
Belgi, Alessia   +11 more
core   +1 more source

α-Conotoxin ImI Incorporating Stable Cystathionine Bridges Maintains Full Potency and Identical Three-Dimensional Structure

open access: yes, 2016
The two disulfide bonds of α-conotoxin ImI, a peptide antagonist of the α7 nicotinic acetylcholine receptor (nAChR), were systematically replaced with isosteric redox-stable cystathionine thioethers. Regioselective thioether formation was accomplished on
Paul F. Alewood (1520788)   +5 more
core   +2 more sources

Solution conformation of α-conotoxin GIC, a novel potent antagonist of α3β2 nicotinic acetylcholine receptors

open access: yes, 2004
α-Conotoxin GIC is a 16-residue peptide isolated from the venom of the cone snail Conus geographus. α-Conotoxin GIC potently blocks the α3β2 subtype of human nicotinic acetylcholine receptor, showing a high selectivity for neuronal versus muscle subtype [
Do-Hyoung Kim   +4 more
core   +1 more source

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