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Three-dimensional structure of the alpha-conotoxin EI determined by proton NMR spectroscopy
Title
Three-dimensional structure of the alpha-conotoxin EI determined by proton NMR spectroscopy.
Creator
Franco, Aldo, Florida Atlantic University, Mari, Frank
Abstract/Description
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
1998
PURL
http://purl.flvc.org/fcla/dt/15609
Subject Headings
Conus--Venom, Peptides--Structure, Nuclear magnetic resonance spectroscopy
Format
Document (PDF)
Conopeptidomics of Conus regius
Title
Conopeptidomics of Conus regius.
Creator
Franco, Aldo, Florida Atlantic University, Charles E. Schmidt College of Science, Department of Chemistry and Biochemistry
Abstract/Description
The main objective of this dissertation is the isolation and characterization of novel neuroactive peptides from Conus regius. The conopeptides targeted in this work have a MW of 3500 Da or less, in the hopes that they can become viable drug candidates. A total of 30 sequences were isolated and characterized from the venom of Conus regius, giving us a partial library of the conopeptides found in this species. Techniques such as size exclusion chromatography, reversed phase chromatography,...
Show moreThe main objective of this dissertation is the isolation and characterization of novel neuroactive peptides from Conus regius. The conopeptides targeted in this work have a MW of 3500 Da or less, in the hopes that they can become viable drug candidates. A total of 30 sequences were isolated and characterized from the venom of Conus regius, giving us a partial library of the conopeptides found in this species. Techniques such as size exclusion chromatography, reversed phase chromatography, mass spectrometry, nano-nuclear magnetic resonance, chemical modifications of peptides, peptide sequencing through Edman degradation and in some instances bioassays were used together in an effort to perform "conopeptidomics" of Conus regius. The first chapter deals with Conus regius M-superfamily conopeptides. The second chapter is about the A-superfamily conopeptides found in Conus regius. The third chapter deals with Conus regius P-superfamily conopeptides. Finally the fourth chapter encompasses the T-superfamily conopeptides and all other small and linear peptides found in Conus regius that do not have a classification. This work is the first example reported, for any cone snail species, where most of the components of the venom have been sequenced directly for a single cone snail species. This work shows that a more realistic library of conopeptides can be obtained by direct analysis of the venom as opposed to cDNA libraries, which while useful; it does not reflect the post-translational modifications commonly found in conopeptides.
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Date Issued
2006
PURL
http://purl.flvc.org/fcla/dt/12206
Subject Headings
Chemistry, Biochemistry
Format
Document (PDF)