Results 31 to 40 of about 925,689 (154)
Solution structure of α-conotoxin SI [PDF]
, 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
Residues Responsible for the Selectivity of α-Conotoxins for Ac-AChBP or nAChRs
Marine Drugs, 2016 Nicotinic acetylcholine receptors (nAChRs) are targets for developing new drugs to treat severe pain, nicotine addiction, Alzheimer disease, epilepsy, etc. α-Conotoxins are biologically and chemically diverse. With 12–19 residues and two disulfides, they
Bo Lin, Shihua Xiang, Mengsen Li
doaj +1 more source
Design of New α-Conotoxins: From Computer Modeling to Synthesis of Potent Cholinergic Compounds
Marine Drugs, 2011 A series of 14 new analogs of α-conotoxin PnIA Conus pennaceus was synthesized and tested for binding to the human α7 nicotinic acetylcholine receptor (nAChR) and acetylcholine-binding proteins (AChBP) Lymnaea stagnalis and Aplysia californica.
Alexey Y. Khruschov +3 more
doaj +1 more source
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 +6 more
doaj +1 more source
SPIDR: small-molecule peptide-influenced drug repurposing
BMC Bioinformatics, 2018 Background Conventional de novo drug design is costly and time consuming, making it accessible to only the best resourced research organizations. An emergent approach to new drug development is drug repurposing, in which compounds that have already gone ...
Matthew D. King +4 more
doaj +1 more source
Protein & Cell, 2017 In the original publication of the article the keywords are incorrectly online published. The correct keywords should read as α-Conotoxin; Nicotinc acetylcholine receptor; Acetylcholine binding protein; X-ray crystallography”.
Manyu Xu +5 more
doaj +1 more source
Unravelling the allosteric binding mode of αD-VxXXB at nicotinic acetylcholine receptors
Frontiers in Pharmacology, 2023 αD-conotoxins are 11 kDa homodimers that potently inhibit nicotinic acetylcholine receptors (nAChRs) through a non-competitive (allosteric) mechanism. In this study, we describe the allosteric binding mode of the granulin-like C-terminal (CTD) of VxXXB ...
Thao NT Ho +2 more
doaj +1 more source
Structural mechanisms for α-conotoxin activity at the human α3β4 nicotinic acetylcholine receptor
, 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
Frontiers in Pharmacology, 2019 Peptides derived from animal venoms provide important research tools for biochemical and pharmacological characterization of receptors, ion channels, and transporters.
Yamina El Hamdaoui +10 more
doaj +1 more source
Solution Structure and Acid-Base Properties of Reduced α-Conotoxin MI [PDF]
, 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