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ScrepYard: An online resource for disulfide-stabilized tandem repeat peptides
Journal article   Open access   Peer reviewed

ScrepYard: An online resource for disulfide-stabilized tandem repeat peptides

Junyu Liu, Michael Maxwell, Thom Cuddihy, Theo Crawford, Madeline Bassetti, Cameron Hyde, Steve Peigneur, Jan Tytgat, Eivind A B Undheim and Mehdi Mobli
Protein Science, Vol.32(2), pp.1-12
2023
PMCID: PMC9885460
PMID: 36644825
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ScrepYard An online resource for disulfide-stabilizedtandem repeat peptides2.37 MBDownloadView
Published Version Open Access CC BY-NC-ND V4.0

Abstract

SCREPs bioactive bivalent disulfide-rich multivalent peptide secreted proteins tandem-repeat
Receptor avidity through multivalency is a highly sought-after property of ligands. While readily available in nature in the form of bivalent antibodies, this property remains challenging to engineer in synthetic molecules. The discovery of several bivalent venom peptides containing two homologous and independently folded domains (in a tandem repeat arrangement) has provided a unique opportunity to better understand the underpinning design of multivalency in multimeric biomolecules, as well as how naturally occurring multivalent ligands can be identified. In previous work, we classified these molecules as a larger class termed secreted cysteine rich repeat proteins (SCREPs). Here, we present an online resource; ScrepYard, designed to assist researchers in identification of SCREP sequences of interest and to aid in characterizing this emerging class of biomolecules. Analysis of sequences within the ScrepYard reveals that two domain tandem repeats constitute the most abundant SCREP domain architecture, while the interdomain "linker" regions connecting the functional domains are found to be abundant in amino acids with short or polar sidechains and contain an unusually high abundance of proline residues. Finally, we demonstrate the utility of ScrepYard as a virtual screening tool for discovery of putatively multivalent peptides, by using it as a resource to identify a previously uncharacterized serine protease inhibitor and confirm its predicted activity using an enzyme assay.

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