A Naturally Occurring Peptide with an Elementary Single Disulfide-Directed β-Hairpin Fold

Structure
Samuel D RobinsonRaymond S Norton

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 have designated the single disulfide-directed β hairpin (SDH). The SDH fold is highly resistant to thermal denaturation and forms the core of several other multiple disulfide-containing peptide folds, including the inhibitor cystine knot. This elementary fold may offer a valuable starting point for the design and engineering of new bioactive peptides.

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Citations

Jan 13, 2017·Journal of Peptide Science : an Official Publication of the European Peptide Society·Ersilia NigroAntonello Pessi
Apr 12, 2017·Expert Opinion on Drug Discovery·Raymond S Norton
Feb 14, 2018·The Journal of Experimental Biology·Kellen DeLaneyLingjun Li
Apr 25, 2017·Biochemistry·Balasubramanyam ChittoorRaymond S Norton
Feb 6, 2017·Journal of Proteome Research·Marimuthu VijayasarathyPadmanabhan Balaram
Oct 22, 2019·Chemical Reviews·Ai-Hua JinPaul F Alewood

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