Sabareesh, V and Gowd, Hanumae K and Ramasamy, P and Sudarslal, S and Krishnan, KS and Sikdar, SK and Balaram, P (2006) Characterization of contryphans from Conus loroisii and Conus amadis that target calcium channels. In: Peptides, 27 (11). pp. 2647-2654.
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Abstract
Distinctly different effects of two closely related contryphans have been demonstrated on voltage-activated $Ca^{2+}$ channels. The peptides Lo959 and Am975 were isolated from Conus loroisii, a vermivorous marine snail and Conus amadis, a molluscivore, respectively. The sequences of Lo959 and Am975 were deduced by mass spectrometric sequencing (MALDI-MS/MS) and confirmed by chemical synthesis. The sequences of Lo959, $GCP^D WDPWC-NH_2$ and Am975, $GCO^D WDPWC-NH_2$ (O: 4-trans-hydroxyproline: Hyp), differ only at residue 3; Pro in Lo959, Hyp in Am975, which is identical to contryphan-P, previously isolated from Conus purpurascens, a piscivore; while Lo959 is a novel peptide. Both Lo959 and Am975 undergo slow conformational interconversion under reverse-phase chromatographic conditions, a characteristic feature of all contryphans reported thus far. Electrophysiological studies performed using dorsal root ganglion neurons reveal that both peptides target high voltage-activated $Ca^{2+}$ channels. While Lo959 increases the $Ca^{2+}$ current, Am975 causes inhibition. The results establish that subtle sequence effects, which accompany post-translational modifications in Conus peptides, can have dramatic effects on target ion channels.
Item Type: | Journal Article |
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Publication: | Peptides |
Publisher: | Elsevier |
Additional Information: | Copyright of this article belongs to Elsevier. |
Keywords: | Cone snails;Contryphans;Post-translational modifications;Slow conformational interconversion;DRG neurons, Voltage-activated calcium channels; |
Department/Centre: | Division of Biological Sciences > Molecular Biophysics Unit |
Date Deposited: | 16 May 2008 |
Last Modified: | 23 Jan 2013 09:13 |
URI: | http://eprints.iisc.ac.in/id/eprint/13988 |
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