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  • Title: Isolation and characterization of α-conotoxin LsIA with potent activity at nicotinic acetylcholine receptors.
    Author: Inserra MC, Kompella SN, Vetter I, Brust A, Daly NL, Cuny H, Craik DJ, Alewood PF, Adams DJ, Lewis RJ.
    Journal: Biochem Pharmacol; 2013 Sep 15; 86(6):791-9. PubMed ID: 23924607.
    Abstract:
    A new α-conotoxin LsIA was isolated from the crude venom of Conus limpusi using assay-guided RP-HPLC fractionation. Synthetic LsIA was a potent antagonist of α3β2, α3α5β2 and α7 nAChRs, with half-maximal inhibitory concentrations of 10, 31 and 10 nM, respectively. The structure of LsIA determined by NMR spectroscopy comprised a characteristic disulfide bond-stabilized α-helical structure and disordered N-terminal region. Potency reductions of up to 9-fold were observed for N-terminally truncated analogues of LsIA at α7 and α3β2 nAChRs, whereas C-terminal carboxylation enhanced potency 3-fold at α3β2 nAChRs but reduced potency 3-fold at α7 nAChRs. This study gives further insight into α-conotoxin pharmacology and the molecular basis of nAChR selectivity, highlighting the influence of N-terminal residues and C-terminal amidation on conotoxin pharmacology.
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