Current Search: Conus--Venom (x)
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Title
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Variability in the venom of Conus regius.
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Creator
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Uribe-Benninghoff, Alejandro., Florida Atlantic University, Hartmann, James X., Mari, Frank
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Abstract/Description
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The venom of two different geographical populations of Conus regius has been isolated and characterized. Comparisons between the chromatographic profiles of the venom of these two populations exhibited similarities and differences among the venom's constituents. MALDI-TOF and PCR analysis techniques ratified the differences present in the venom of both populations. It is postulated that these differences could reflect the rapid adaptive nature of cone snails in an actual stage of speciation....
Show moreThe venom of two different geographical populations of Conus regius has been isolated and characterized. Comparisons between the chromatographic profiles of the venom of these two populations exhibited similarities and differences among the venom's constituents. MALDI-TOF and PCR analysis techniques ratified the differences present in the venom of both populations. It is postulated that these differences could reflect the rapid adaptive nature of cone snails in an actual stage of speciation. Molecular weights of the venom's constituents were compared with those of patented conopeptides in the Swiss Protein Database. Results of this comparison indicated that a number of the peptides isolated for both of the populations of C. regius had the same molecular weight as other patented conopeptides. In combination with the PCR analysis of these conopeptides, it has been proposed that some of the venom constituents of the venom of C. regius could have pharmacological applications for vertebrate systems.
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Date Issued
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1999
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PURL
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http://purl.flvc.org/fcla/dt/15746
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Subject Headings
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Conus--Venom
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Format
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Document (PDF)
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Title
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Three-dimensional structure of the alpha-conotoxin EI determined by proton NMR spectroscopy.
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Creator
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Franco, Aldo, Florida Atlantic University, Mari, Frank
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Abstract/Description
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The alpha-conotoxin EI is an 18-residue peptide (RDOCCYHPTCNMSNPQIC; 4-10, 5-18) isolated from the venom of Conus ermineus. This peptide targets the nicotinic acetylcholine receptor (nAChR) found in mammalian skeletal muscle and the electric organ of Torpedo. 2D-NMR methods and dynamical simulated annealing protocols have been used to determine the 3D structure of EI. 133 NOE-derived distances were used to produce 13 structures with minimum energy that complied with the NOE restraints. The...
Show moreThe alpha-conotoxin EI is an 18-residue peptide (RDOCCYHPTCNMSNPQIC; 4-10, 5-18) isolated from the venom of Conus ermineus. This peptide targets the nicotinic acetylcholine receptor (nAChR) found in mammalian skeletal muscle and the electric organ of Torpedo. 2D-NMR methods and dynamical simulated annealing protocols have been used to determine the 3D structure of EI. 133 NOE-derived distances were used to produce 13 structures with minimum energy that complied with the NOE restraints. The structure of EI is characterized by a helical loop between T9 and M12 that is stabilized by the C4-C10 disulfide bond and turns involving C4-C5 and N14-P15. The overall fold of EI is similar to that of other alpha4/7 conotoxins (PnIA/B, MII, EpI). However, unlike these other alpha4/7 conotoxins, EI targets the muscular type nAChR. The differences in selectivity can be attributed to the surface charge distribution among these alpha4/7 conotoxins.
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Date Issued
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1998
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PURL
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http://purl.flvc.org/fcla/dt/15609
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Subject Headings
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Conus--Venom, Peptides--Structure, Nuclear magnetic resonance spectroscopy
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Format
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Document (PDF)
