Journal article
A Naturally Occurring Peptide with an Elementary Single Disulfide-Directed β-Hairpin Fold
SD Robinson, S Chhabra, A Belgi, B Chittoor, H Safavi-Hemami, AJ Robinson, AT Papenfuss, AW Purcell, RS Norton
Structure | Published : 2016
Abstract
Certain peptide folds, owing to a combination of intrinsic stability and resilience to amino acid substitutions, are particularly effective for the display of diverse functional groups. Such "privileged scaffolds" are valuable as starting points for the engineering of new bioactive molecules. We have identified a precursor peptide expressed in the venom gland of the marine snail Conus victoriae, which appears to belong to a hitherto undescribed class of molluscan neuropeptides. Mass spectrometry matching with the venom confirmed the complete mature peptide sequence as a 31-residue peptide with a single disulfide bond. Solution structure determination revealed a unique peptide fold that we ha..
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Awarded by State Government of Victoria
Funding Acknowledgements
We thank Johan Pas for specimen collection and Dr. Nicholas Williamson for technical assistance with MS. We thank Dr. Yee-Foong Mok for technical assistance with analytical ultracentrifugation and CD spectroscopy. The authors acknowledge financial support from a Discovery Grant (DP110101331) from the Australian Research Council (A.W.P.). A.W.P. and R.S.N. acknowledge fellowship support from the Australian National Health and Medical Research Council (NHMRC). A.T.P. was supported by an NHMRC Career Development Fellowship (1003856) and a Program Grant (1054618), and benefited from support by the Victorian State Government Operational Infrastructure Support and Australian Government NHMRC Independent Research Institute Infrastructure Support Scheme. H.S-H. is supported by a Marie Curie Fellowship from the European Commission (CONBIOS 330486). S.D.R. received support from a Monash University Postgraduate Publications Award.