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Plant cyclotides: A unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural motif.
The structural features of the two apparent subfamilies of the CCK peptides which may be significant for the likely defense related role of these peptides within plants are defined.
Novel ω-Conotoxins from Conus catus Discriminate among Neuronal Calcium Channel Subtypes*
In electrophysiological studies, ω-conotoxins CVID and MVIIA had similar potencies to inhibit current through central and peripheral splice variants of the rat N-type calcium channels when coexpressed with rat β3 in Xenopus oocytes, but the potency of CVID increased when α1B-d and α1b-b were expressed in the absence of ratβ3.
Structure-activity relationships of omega-conotoxins MVIIA, MVIIC and 14 loop splice hybrids at N and P/Q-type calcium channels.
A preliminary pharmacophore is developed based on the omega-conotoxin residues most likely to interact with the N-type VSCC, which makes the greatest contribution to VSCC subtype selectivity.
Isolation and characterization of conopeptides by high-performance liquid chromatography combined with mass spectrometry and tandem mass spectrometry.
The sensitivity of mass spectrometry combined with the separatory power of high-performance liquid chromatography was used to investigate the venom of individual cone shells, This analysis has
alpha-conotoxin EpI, a novel sulfated peptide from Conus episcopatus that selectively targets neuronal nicotinic acetylcholine receptors.
Results indicate that EpI and [Tyr15]EpI selectively inhibit alpha3beta2 and alpha3 beta4 nicotinic acetylcholine receptors.
α-Conotoxin EpI, a Novel Sulfated Peptide from Conus episcopatus That Selectively Targets Neuronal Nicotinic Acetylcholine Receptors*
Results indicate that EpI and [Tyr15]EpI selectively inhibit α3β2 and α3 β4 nicotinic acetylcholine receptors.