Results 21 to 30 of about 1,087 (186)

Redox-Active Conopeptide Li520 Has Evolved to Catalyze Oxidative Folding of Conotoxins [PDF]

open access: yesACS Omega
Shweta Dhannura   +8 more
doaj   +2 more sources

The macrocycle inhibitor landscape of SLC-transporter. [PDF]

open access: yesMol Inform
Abstract In the past years the interest in Solute Carrier Transporters (SLC) has increased due to their potential as drug targets. At the same time, macrocycles demonstrated promising activities as therapeutic agents. However, the overall macrocycle/SLC‐transporter interaction landscape has not been fully revealed yet.
Granulo N, Sosnin S, Digles D, Ecker GF.
europepmc   +2 more sources

Hormone-like conopeptides - new tools for pharmaceutical design. [PDF]

open access: yesRSC Med Chem, 2020
Marine cone snails produce an array of hormone-like peptides in their venom, providing bioactive leads for developing peptide drugs and small molecule mimetics.
Turner A, Kaas Q, Craik DJ.
europepmc   +5 more sources

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

open access: yesAngewandte 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   +8 more
wiley   +2 more sources

Diversity of Conopeptides and Conoenzymes from the Venom Duct of the Marine Cone Snail Conus bayani as Determined from Transcriptomic and Proteomic Analyses

open access: yesMarine Drugs, 2021
Marine cone snails are predatory gastropods characterized by a well-developed venom apparatus and highly evolved hunting strategies that utilize toxins to paralyze prey and defend against predators.
Rajesh Rajaian Pushpabai   +4 more
doaj   +1 more source

Diversity and Novelty of Venom Peptides in Vermivorous Cone Snails, Subgenus <i>Rhizoconus</i> (Gastropoda: Mollusca). [PDF]

open access: yesMar Drugs
A large majority of cone snails (a species in the genus Conus) are vermivorous (worm-hunting), but the diversity and bioactivity of their venom peptides remain largely unexplored.
Florece CMC   +3 more
europepmc   +3 more sources

Cupryphans, metal‐binding, redox‐active, redesigned conopeptides [PDF]

open access: yesProtein Science, 2009
AbstractContryphans are bioactive peptides, isolated from the venom of marine snails of the genus Conus, which are characterized by the short length of the polypeptide chain and the high degree of unusual post‐translational modifications. The cyclization of the polypeptide chain through a single disulphide bond, the presence of two conserved Pro ...
BARBA, MARCO   +7 more
openaire   +6 more sources

Characterisation of a Novel A-Superfamily Conotoxin

open access: yesBiomedicines, 2020
Conopeptides belonging to the A-superfamily from the venomous molluscs, Conus, are typically α-conotoxins. The α-conotoxins are of interest as therapeutic leads and pharmacological tools due to their selectivity and potency at nicotinic acetylcholine ...
David T. Wilson   +6 more
doaj   +1 more source

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

open access: yesActa 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   +3 more
wiley   +1 more source

Tyrosine-rich Conopeptides Affect Voltage-gated K+ Channels [PDF]

open access: yesJournal 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. The peptides have no disulfide cross-links and are 30 amino acids long; the high content of tyrosine is unprecedented for any native ...
Imperial, Julita S.   +7 more
openaire   +4 more sources

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