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Toxins 2018, 10(11), 437;

Nuclear Magnetic Resonance seq (NMRseq): A New Approach to Peptide Sequence Tags

Centre for Biodiscovery and Molecular Development of Therapeutics, AITHM, James Cook University, Cairns, QLD 4870, Australia
Author to whom correspondence should be addressed.
Received: 14 October 2018 / Accepted: 25 October 2018 / Published: 28 October 2018
(This article belongs to the Special Issue Emerging Marine Biotoxins)
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Structural analysis of peptides with nuclear magnetic resonance (NMR) spectroscopy generally relies on knowledge of the primary sequence to enable assignment of the resonances prior to determination of the three-dimensional structure. Resonance assignment without knowledge of the sequence is complicated by redundancy in amino acid type, making complete de novo sequencing using NMR spectroscopy unlikely to be feasible. Despite this redundancy, we show here that NMR spectroscopy can be used to identify short sequence tags that can be used to elucidate full-length peptide sequences via database searching. In the current study, we have used this approach to identify conotoxins from the venom of the cone snail Conus geographus and determined the three-dimensional structure of a member of the I3 superfamily. This approach is most likely to be useful for the characterization of disulfide-rich peptides, such as those that were chosen for this study, as they generally have well-defined structures, which enhances the quality of the NMR spectra. In contrast to other sequencing methods, the lack of sample manipulation, such as protease digestion, allows for subsequent bioassays to be carried out using the native sample used for sequence identification. View Full-Text
Keywords: NMR spectroscopy; disulfide-rich peptide; conotoxin NMR spectroscopy; disulfide-rich peptide; conotoxin

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Wilson, D.; Daly, N.L. Nuclear Magnetic Resonance seq (NMRseq): A New Approach to Peptide Sequence Tags. Toxins 2018, 10, 437.

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