Results 1 to 10 of about 917,242 (94)

Degradation kinetics of α-conotoxin TxID [PDF]

open access: yesFEBS Open Bio, 2019
α‐Conotoxin (CTx) TxID is a potent α3β4 nicotinic acetylcholine receptor (nAChR) antagonist that has been suggested as a potential drug candidate to treat addiction and small cell lung cancer.
Dongting Zhangsun, Sulan Luo, Sulan Luo
exaly   +5 more sources

Loop2 Size Modification Reveals Significant Impacts on the Potency of α-Conotoxin TxID [PDF]

open access: yesMarine Drugs, 2023
α4/6-conotoxin TxID, which was identified from Conus textile, simultaneously blocks rat (r) α3β4 and rα6/α3β4 nicotinic acetylcholine receptors (nAChRs) with IC50 values of 3.6 nM and 33.9 nM, respectively.
Dongting Zhangsun   +2 more
exaly   +5 more sources

Fluorescently Labeled α-Conotoxin TxID, a New Probe for α3β4 Neuronal Nicotinic Acetylcholine Receptors [PDF]

open access: yesMarine Drugs, 2022
Neuronal nicotinic acetylcholine receptors (nAChRs) are important ion channel membrane proteins that are widely distributed in the central nervous system (CNS) and peripheral nervous system (PNS).
Dongting Zhangsun   +2 more
exaly   +5 more sources

DSPE-PEG Modification of α-Conotoxin TxID [PDF]

open access: yesMarine Drugs, 2019
In order to improve stability of a peptide marine drug lead, α-conotoxin TxID, we synthesized and modified TxID at the N-terminal with DSPE-PEG-NHS by a nucleophilic substitution reaction to prepare the DSPE-PEG-TxID for the first time. The reaction
Dongting Zhangsun, Sulan Luo, Sulan Luo
exaly   +5 more sources

α-Conotoxin TxID and [S9K]TxID, α3β4 nAChR Antagonists, Attenuate Expression and Reinstatement of Nicotine-Induced Conditioned Place Preference in Mice [PDF]

open access: yesMarine Drugs, 2020
Tobacco smoking has become a prominent health problem faced around the world. The α3β4 nicotinic acetylcholine receptor (nAChR) is strongly associated with nicotine reward and withdrawal symptom.
Dongting Zhangsun, Sulan Luo, Jinpeng Yu
exaly   +5 more sources

Effect of Methionine Oxidation and Substitution of α-Conotoxin TxID on α3β4 Nicotinic Acetylcholine Receptor [PDF]

open access: yesMarine Drugs, 2018
α-Conotoxin TxID was discovered from Conus textile by gene cloning, which has 4/6 inter-cysteine loop spacing and selectively inhibits α3β4 nicotinic acetylcholine receptor (nAChR) subtype.
Rui Li, Dongting Zhangsun, Jie Ren
exaly   +5 more sources

Hippocampal Metabolomics Reveal the Mechanism of α-Conotoxin [S9K]TxID Attenuating Nicotine Addiction [PDF]

open access: yesMarine Drugs
Nicotine is the main substance responsible for the development of tobacco addiction. The α3β4 nicotinic acetylcholine receptors (nAChRs) are a potential key target for mitigating nicotine reward.
Cheng Cui   +2 more
exaly   +5 more sources

Characterization of a Novel α-Conotoxin TxID from Conus textile That Potently Blocks Rat α3β4 Nicotinic Acetylcholine Receptors [PDF]

open access: yesJournal of Medicinal Chemistry, 2013
The alpha 3 beta 4 nAChRs are implicated in pain sensation in the PNS and addiction to nicotine in the CNS. We identified an alpha-4/6-conotoxin (CTx) TxID from Conus textile.
Dongting Zhangsun   +2 more
exaly   +4 more sources

Computational Design of α-Conotoxins to Target Specific Nicotinic Acetylcholine Receptor Subtypes. [PDF]

open access: yesChemistry
FoldX 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]

open access: yesJ Pept Sci
This 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

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