Results 31 to 40 of about 849 (177)

Tyrosine-rich conopeptides affect voltage-gated K+ channels [PDF]

Journal of Biological Chemistry, 2008
Two venom peptides, CPY-Pl1 (EU000528) and CPY-Fe1 (EU000529), characterized from the vermivorous marine snails Conus planorbis and Conus ferrugineus, define a new class of conopeptides, the conopeptide Y (CPY) family.
Sporning, Annett, Craik, D., Alewood, Paul F., Terlau, Heinrich, Sporning, A., Daly, N., Craik, David J., Olivera, Baldomero M., Chen, P., Terlau, H., Chen, Ping, Alewood, P., Imperial, Julita S., Olivera, Baldormero M., Imperial, J., Daly, Norelle L., Olivera, B.   +16 more
core   +8 more sources

Determination of disulfide bridge pattern in ω-conopeptides

International Journal of Peptide and Protein Research, 1995
Synthetic versions of seven naturally occurring omega-conopeptides were subjected to structural analyses in order to determine their disulfide bridge pattern.
Gaur, Smita, Nadasdi, Laszlo, Ramachandran, J., Chung, David, Bell, John R.   +4 more
core   +3 more sources

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 ...
Daly, N. L., Craik, David J.
core   +5 more sources

Predatory and Defensive Strategies in Cone Snails [PDF]

Toxins
Cone snails are carnivorous marine animals that prey on fish (piscivorous), worms (vermivorous), or other mollusks (molluscivorous). They produce a complex venom mostly made of disulfide-rich conotoxins and conopeptides in a compartmentalized venom gland.
Zahrmina Ratibou, Nicolas Inguimbert, Sébastien Dutertre   +2 more
doaj   +2 more sources

Conformational Heterogeneity of Pro–Pro Containing 23-Membered Ring Conopeptides by NMR [PDF]

ACS Omega
Pooja Dhurjad, Srinivas Reddy Dannarm, Khajapeer Shaik, Parita Wanjari, Rajesh Sonti   +4 more
doaj   +2 more sources

A Chemoenzymatic Approach To Produce a Cyclic Analogue of the Analgesic Drug MVIIA (Ziconotide)

Angewandte Chemie, Volume 135, Issue 29, July 17, 2023., 2023
A chemoenzymatic method has been developed to prepare backbone cyclic analogues of the ω‐conotoxin MVIIA. The most potent cyclic analogue, cM‐7, shows highly improved stability and maintains the activity of the native peptide. Abstract Ziconotide (ω‐conotoxin MVIIA) is an approved analgesic for the treatment of chronic pain.
Yan Zhou, Peta J. Harvey, Johannes Koehbach, Lai Yue Chan, Alun Jones, Åsa Andersson, Irina Vetter, Thomas Durek, David J. Craik   +8 more
wiley   +2 more sources

Improved prediction of conopeptide superfamilies with ConoDictor 2.0. [PDF]

Bioinform Adv, 2021
Abstract Motivation Cone snails are among the richest sources of natural peptides with promising pharmacological and therapeutic applications. With the reduced costs of RNAseq, scientists now heavily rely on venom gland transcriptomes for the mining of novel bioactive conopeptides, but the ...
Koua D, Ebou A, Dutertre S.
europepmc   +3 more sources

Side‐chain dynamics of the α1B‐adrenergic receptor determined by NMR via methyl relaxation

Protein Science, Volume 32, Issue 11, November 2023., 2023
Abstract G protein‐coupled receptors (GPCRs) are medically important membrane proteins that sample inactive, intermediate, and active conformational states characterized by relatively slow interconversions (~μs–ms). On a faster timescale (~ps–ns), the conformational landscape of GPCRs is governed by the rapid dynamics of amino acid side chains.
Christian Baumann, Wan‐Chin Chiang, Renato Valsecchi, Simon Jurt, Mattia Deluigi, Matthias Schuster, Karl Johan Rosengren, Andreas Plückthun, Oliver Zerbe   +8 more
wiley   +1 more source

High‐resolution crystal structure of the Mu8.1 conotoxin from Conus mucronatus

Acta Crystallographica Section F, Volume 79, Issue 9, Page 240-246, September 2023., 2023
The crystal structure of the Mu8.1 conotoxin was determined in the high‐symmetry space group I4122 at 1.67 Å resolution. This crystal structure reveals a surface‐exposed Zn2+‐binding site and establishes a hydrogen‐bonding network around Lys55 buried at the dimer interface.Marine cone snails produce a wealth of peptide toxins (conotoxins) that bind ...
Emilie Müller, Celeste Menuet Hackney, Lars Ellgaard, Jens Preben Morth   +3 more
wiley   +1 more source

Isolation and structural identification of a new T1-conotoxin with unique disulfide connectivities derived from Conus bandanus [PDF]

Journal of Venomous Animals and Toxins including Tropical Diseases, 2020
Background: Conopeptides are neuropharmacological peptides derived from the venomous salivary glands of cone snails. Among 29 superfamilies based on conserved signal sequences, T-superfamily conotoxins, which belong to the smallest group, include four ...
Nguyen Bao, Jean-Pière Lecaer, Ngo Dang Nghia, Phan Thi Khanh Vinh   +3 more
doaj   +1 more source