Results 161 to 170 of about 1,281 (179)

Conopeptides as novel options for pain management

Drugs of the Future, 2011
Conopeptides are the peptidic components of the venoms of marine cone snails from the Conus genus. Aside from their natural function in pharmacologically immobilizing prey, they have attracted the attention of drug designers in recent years because of their potency and selectivity at a range of pharmaceutically important targets in mammals, including ...
Daly, N. L., Craik, David J.
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Cardiovascular Effects of ω-Conopeptides in Conscious Rats: Mechanisms of Action

Journal of Cardiovascular Pharmacology, 1992
We examined the effects of omega-conopeptides, a novel class of neuronal voltage-gated calcium channel antagonists, on hemodynamic responses in rats. Intravenous (i.v.) injections of SNX-111 (omega-conopeptide MVIIA) dose-dependently decreased arterial blood pressure (BP) in conscious rats. Intracerebroventricular (i.c.v.) SNX-111 injections (580 pmol)
S. Scott Bowersox, Tejinder Singh, Laszlo Nadasdi, Zofia Zukowska-Grojec, Karen Valentino, Brian B. Hoffman   +5 more
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Novel conopeptides in a form of disulfide-crosslinked dimer

Peptides, 2010
In our present work, seven conotoxins and conopeptides were cloned from four cone snail species based on the M-superfamily signal peptides. Among them, two conopeptides, Vt3.1 and Vt3.2, showed unusual sequence characteristics. Both of them contained two cysteines that are separated by just one non-cysteine residue. In vitro, the chemically synthesized
Xue-Chen, Wu, Mi, Zhou, Can, Peng, Xiao-Xia, Shao, Zhan-Yun, Guo, Cheng-Wu, Chi   +5 more
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Identification and classification of conopeptides using profile Hidden Markov Models

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2012
Conopeptides are small toxins produced by predatory marine snails of the genus Conus. They are studied with increasing intensity due to their potential in neurosciences and pharmacology. The number of existing conopeptides is estimated to be 1 million, but only about 1000 have been described to date.
Silja, Laht, Dominique, Koua, Lauris, Kaplinski, Frédérique, Lisacek, Reto, Stöcklin, Maido, Remm   +5 more
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Conopeptides from Conus striatus and Conus textile by cDNA cloning☆

Peptides, 1999
Conopeptide content in Conus textile and Conus striatus venoms were examined by polymerase chain reaction amplification of alpha-conopeptide cDNA and rapid amplification of 3' cDNA ends of O-superfamily conopeptide cDNA. Two new alpha-conopeptide sequences and six new O-superfamily conopeptide sequences from C.
B S, Lu, F, Yu, D, Zhao, P T, Huang, C F, Huang   +4 more
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Oxidative Folding of Conopeptides Modified by Conus Protein Disulfide Isomerase

The Protein Journal, 2017
Protein disulfide isomerase is a type of enzyme that catalyses the oxidation, isomerization and reduction of disulfide bonds. Conotoxins that containing disulfide bonds are likely substrates of protein disulfide isomerise. Here, we cloned 12 protein disulfide isomerise genes from 12 different cone snail species that inhabited the sea near Sanya in ...
Lei, Wang, Xiaomin, Wang, Zhenghua, Ren, Wei, Tang, Qiong, Zou, Jinxing, Wang, Shangwu, Chen, Han, Zhang, Anlong, Xu   +8 more
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Molecular interaction of δ-conopeptide EVIA with voltage-gated Na+ channels

Biochimica et Biophysica Acta (BBA) - General Subjects, 2016
Abstract Background For a large number of conopeptides basic knowledge related to structure-activity relationships is unavailable although such information is indispensable with respect to drug development and their use as drug leads. Methods A combined experimental and theoretical approach employing electrophysiology and molecular modeling was ...
Daniel Tietze, Enrico Leipold, Pascal Heimer, Miriam Böhm, Wadim Winschel, Diana Imhof, Stefan H. Heinemann, Alesia A. Tietze   +7 more
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Structure of the O‐Glycosylated Conopeptide CcTx from Conus consors Venom

Chemistry – A European Journal, 2012
AbstractThe glycopeptide CcTx, isolated from the venom of the piscivorous cone snail Conus consors, belongs to the κA‐family of conopeptides. These toxins elicit excitotoxic responses in the prey by acting on voltage‐gated sodium channels. The structure of CcTx, a first in the κA‐family, has been determined by high‐resolution NMR spectroscopy together ...
Hocking, H.G., Gerwig, G.J., Dutertre, S., Violette, A., Favreau, P., Stöcklin, R., Kamerling, J.P., Boelens, R.   +7 more
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Structure-aided function assignment to the transcriptomic conopeptide Am931

Toxicon
Implementation of the next-generation technologies for gene sequencing of venom duct transcriptome has provided a large number of peptide sequences of marine cone snails. Emerging technologies on computational platforms are now rapidly evolving for the accurate predictions of the 3D structure of the polypeptide using the primary sequence.
Shamasoddin, Shekh, Shweta, Dhannura, Pooja, Dhurjad, Challa, Ravali, Spoorti, M M, Sreepriya, Kakkat, , Vishwajyothi, Marimuthu, Vijayasarathy, Rajesh, Sonti, Konkallu Hanumae, Gowd   +9 more
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Two short d-Phe-containing cysteine-free conopeptides from Conus marmoreus

Peptides, 2010
The cysteine-free conopeptides are naturally occurring components of the venom of cone snails and have been relatively less investigated than the cysteine-containing conopeptides. In this work, we used thiol-exchange chromatography to isolate cysteine-free conopeptides from the venom of Conus marmoreus.
Ling, Zhang, Xiaoxia, Shao, Chengwu, Chi, Chunguang, Wang   +3 more
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