TY - JOUR
T1 - Structure and Biological Activity of a Turripeptide from Unedogemmula bisaya Venom
AU - Omaga, Carla A.
AU - Carpio, Louie D.
AU - Imperial, Julita S.
AU - Daly, Norelle L.
AU - Gajewiak, Joanna
AU - Flores, Malem S.
AU - Espino, Samuel S.
AU - Christensen, Sean
AU - Filchakova, Olena M.
AU - López-Vera, Estuardo
AU - Raghuraman, Shrinivasan
AU - Olivera, Baldomero M.
AU - Concepcion, Gisela P.
N1 - Publisher Copyright:
© 2017 American Chemical Society.
Copyright:
Copyright 2017 Elsevier B.V., All rights reserved.
PY - 2017/11/14
Y1 - 2017/11/14
N2 - The turripeptide ubi3a was isolated from the venom of the marine gastropod Unedogemmula bisaya, family Turridae, by bioassay-guided purification; both native and synthetic ubi3a elicited prolonged tremors when injected intracranially into mice. The sequence of the peptide, DCCOCOAGAVRCRFACC-NH2 (O = 4-hydroxyproline) follows the framework III pattern for cysteines (CC-C-C-CC) in the M-superfamily of conopeptides. The three-dimensional structure determined by NMR spectroscopy indicated a disulfide connectivity that is not found in conopeptides with the cysteine framework III: C1-C4, C2-C6, C3-C5. The peptide inhibited the activity of the α9α10 nicotinic acetylcholine receptor with relatively low affinity (IC50, 10.2 μM). Initial Constellation Pharmacology data revealed an excitatory activity of ubi3a on a specific subset of mouse dorsal root ganglion neurons.
AB - The turripeptide ubi3a was isolated from the venom of the marine gastropod Unedogemmula bisaya, family Turridae, by bioassay-guided purification; both native and synthetic ubi3a elicited prolonged tremors when injected intracranially into mice. The sequence of the peptide, DCCOCOAGAVRCRFACC-NH2 (O = 4-hydroxyproline) follows the framework III pattern for cysteines (CC-C-C-CC) in the M-superfamily of conopeptides. The three-dimensional structure determined by NMR spectroscopy indicated a disulfide connectivity that is not found in conopeptides with the cysteine framework III: C1-C4, C2-C6, C3-C5. The peptide inhibited the activity of the α9α10 nicotinic acetylcholine receptor with relatively low affinity (IC50, 10.2 μM). Initial Constellation Pharmacology data revealed an excitatory activity of ubi3a on a specific subset of mouse dorsal root ganglion neurons.
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U2 - 10.1021/acs.biochem.7b00485
DO - 10.1021/acs.biochem.7b00485
M3 - Article
C2 - 29090914
AN - SCOPUS:85034117841
VL - 56
SP - 6051
EP - 6060
JO - Biochemistry
JF - Biochemistry
SN - 0006-2960
IS - 45
ER -