Crystal Structure of the Monomeric Extracellular Domain of α9 Nicotinic Receptor Subunit in Complex With α-Conotoxin RgIA: Molecular Dynamics Insights Into RgIA Binding to α9α10 Nicotinic Receptors [PDF]
Frontiers in Pharmacology, 2019 The α9 subunit of nicotinic acetylcholine receptors (nAChRs) exists mainly in heteropentameric assemblies with α10. Accumulating data indicate the presence of three different binding sites in α9α10 nAChRs: the α9(+)/α9(−), the α9(+)/α10(−), and the α10(+)
Marios Zouridakis +2 more
exaly +4 more sources
Substitution of D-Arginine at Position 11 of α-RgIA Potently Inhibits α7 Nicotinic Acetylcholine Receptor [PDF]
Marine Drugs, 2023 Conotoxins are a class of disulfide-rich peptides found in the venom of cone snails, which have attracted considerable attention in recent years due to their potent activity on ion channels and potential for therapeutics.
Yong Wu, Junjie Zhang, Xiaopeng Zhu
exaly +4 more sources
Engineering Enhanced Antimicrobial Properties in α-Conotoxin RgIA through D-Type Amino Acid Substitution and Incorporation of Lysine and Leucine Residues [PDF]
MoleculesAntimicrobial peptides (AMPs), acknowledged as host defense peptides, constitute a category of predominant cationic peptides prevalent in diverse life forms. This study explored the antibacterial activity of α-conotoxin RgIA, and to enhance its stability
Dongting Zhangsun, Yong Wu, Sulan Luo
exaly +4 more sources
d-Amino Acid Substitution of α-Conotoxin RgIA Identifies its Critical Residues and Improves the Enzymatic Stability [PDF]
Marine Drugs, 2019 α-Conotoxin RgIA is a selective and potent competitive antagonist of rat α9α10 nicotinic acetylcholine receptors (nAChR), but it is much less potent towards human α9α10 nAChR.
Jie Ren +8 more
doaj +2 more sources
From Crystal Structures of RgIA4 in Complex with Ac-AChBP to Molecular Determinants of Its High Potency of α9α10 nAChR [PDF]
Marine Drugs, 2021 α9-containing nicotinic acetylcholine receptors (nAChRs) have been shown to play critical roles in neuropathic pain. The α-conotoxin (α-CTx) RgIA and its analog RgIA4 were identified as the most selective inhibitor of α9α10 nAChR.
Si Pan +5 more
doaj +2 more sources
Interaction of α9α10 Nicotinic Receptors With Peptides and Proteins From Animal Venoms [PDF]
Frontiers in Cellular Neuroscience, 2021 Unlike most neuronal nicotinic acetylcholine receptor (nAChR) subunits, α7, α9, and α10 subunits are able to form functional homo- or heteromeric receptors without any β subunits.
Victor Tsetlin +11 more
doaj +2 more sources
Nicotinic acetylcholine receptors: Therapeutic targets for novel ligands to treat pain and inflammation [PDF]
Pharmacological Research, 2023 Nicotinic acetylcholine receptors (nAChRs) have been historically defined as ligand-gated ion channels and function as such in the central and peripheral nervous systems. Recently, however, non-ionic signaling mechanisms via nAChRs have been demonstrated
Arik J. Hone, J. Michael McIntosh
doaj +2 more sources
Corrigendum: Crystal structure of the monomeric extracellular domain of α9 nicotinic receptor subunit in complex with α-conotoxin RgIA: Molecular dynamics insights into RgIA binding to α9α10 nicotinic receptors [PDF]
Frontiers in Pharmacology, 2022 Marios Zouridakis +9 more
doaj +2 more sources
Computational Design of α-Conotoxins to Target Specific Nicotinic Acetylcholine Receptor Subtypes. [PDF]
ChemistryFoldX was benchmarked as the best energy prediction method, and seven accurate molecular models of α‐conotoxin/nAChRs were developed as surrogates for the experimental complexes. The combined use of FoldX and these molecular models emerged as an effective approach to predict α‐conotoxins with improved pharmaceutical properties.
Wu X +6 more
europepmc +2 more sources
Cyclization of the Analgesic α-Conotoxin Vc1.1 With a Non-Natural Linker: Effects on Structure, Stability, and Bioactivity. [PDF]
J Pept SciThis study cyclized conotoxin Vc1.1 using polyethylene glycol (PEG) linkers of different lengths and demonstrates that linker length modulates the peptide's helicity, thereby influencing its biological activity and stability. ABSTRACT α‐Conotoxin Vc1.1 is a disulfide‐rich peptide and a promising drug candidate for treating neuropathic and chronic pain.
Zhang Y +4 more
europepmc +2 more sources