Lybatides from Lycium barbarum Contain An Unusual Cystine-stapled Helical Peptide Scaffold

Abstract Cysteine-rich peptides (CRPs) of 2–6 kDa are generally thermally and proteolytically stable because of their multiple cross-bracing disulfide bonds. Here, we report the discovery and characterization of two novel cystine-stapled CRPs, designated lybatide 1 and 2 (lyba1 and lyba2), from the...

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Autores principales:	Wei Liang Tan, Ka H. Wong, Jian Lei, Naoki Sakai, Hong Wei Tan, Rolf Hilgenfeld, James P. Tam
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/6bf374fb01a84458acc00e754ce89c4c
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spelling	oai:doaj.org-article:6bf374fb01a84458acc00e754ce89c4c2021-12-02T16:07:02ZLybatides from Lycium barbarum Contain An Unusual Cystine-stapled Helical Peptide Scaffold10.1038/s41598-017-05037-12045-2322https://doaj.org/article/6bf374fb01a84458acc00e754ce89c4c2017-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-05037-1https://doaj.org/toc/2045-2322Abstract Cysteine-rich peptides (CRPs) of 2–6 kDa are generally thermally and proteolytically stable because of their multiple cross-bracing disulfide bonds. Here, we report the discovery and characterization of two novel cystine-stapled CRPs, designated lybatide 1 and 2 (lyba1 and lyba2), from the cortex of Lycium barbarum root. Lybatides, 32 to 33 amino acids in length, are hyperstable and display a novel disulfide connectivity with a cysteine motif of C-C-C-C-CC-CC which contains two pairs of adjacent cysteines (-CC-CC). X-ray structure analysis revealed the presence of a single cystine-stabilized (α + π)-helix in lyba2, a rare feature of CRPs. Together, our results suggest that lybatides, one of the smallest four-disulfide-constrained plant CRPs, is a new family of CRPs. Additionally, this study provides new insights into the molecular diversity of plant cysteine-rich peptides and the unusual lybatide scaffold could be developed as a useful template for peptide engineering and therapeutic development.Wei Liang TanKa H. WongJian LeiNaoki SakaiHong Wei TanRolf HilgenfeldJames P. TamNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-11 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Wei Liang Tan Ka H. Wong Jian Lei Naoki Sakai Hong Wei Tan Rolf Hilgenfeld James P. Tam Lybatides from Lycium barbarum Contain An Unusual Cystine-stapled Helical Peptide Scaffold
description	Abstract Cysteine-rich peptides (CRPs) of 2–6 kDa are generally thermally and proteolytically stable because of their multiple cross-bracing disulfide bonds. Here, we report the discovery and characterization of two novel cystine-stapled CRPs, designated lybatide 1 and 2 (lyba1 and lyba2), from the cortex of Lycium barbarum root. Lybatides, 32 to 33 amino acids in length, are hyperstable and display a novel disulfide connectivity with a cysteine motif of C-C-C-C-CC-CC which contains two pairs of adjacent cysteines (-CC-CC). X-ray structure analysis revealed the presence of a single cystine-stabilized (α + π)-helix in lyba2, a rare feature of CRPs. Together, our results suggest that lybatides, one of the smallest four-disulfide-constrained plant CRPs, is a new family of CRPs. Additionally, this study provides new insights into the molecular diversity of plant cysteine-rich peptides and the unusual lybatide scaffold could be developed as a useful template for peptide engineering and therapeutic development.
format	article
author	Wei Liang Tan Ka H. Wong Jian Lei Naoki Sakai Hong Wei Tan Rolf Hilgenfeld James P. Tam
author_facet	Wei Liang Tan Ka H. Wong Jian Lei Naoki Sakai Hong Wei Tan Rolf Hilgenfeld James P. Tam
author_sort	Wei Liang Tan
title	Lybatides from Lycium barbarum Contain An Unusual Cystine-stapled Helical Peptide Scaffold
title_short	Lybatides from Lycium barbarum Contain An Unusual Cystine-stapled Helical Peptide Scaffold
title_full	Lybatides from Lycium barbarum Contain An Unusual Cystine-stapled Helical Peptide Scaffold
title_fullStr	Lybatides from Lycium barbarum Contain An Unusual Cystine-stapled Helical Peptide Scaffold
title_full_unstemmed	Lybatides from Lycium barbarum Contain An Unusual Cystine-stapled Helical Peptide Scaffold
title_sort	lybatides from lycium barbarum contain an unusual cystine-stapled helical peptide scaffold
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/6bf374fb01a84458acc00e754ce89c4c
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Lybatides from Lycium barbarum Contain An Unusual Cystine-stapled Helical Peptide Scaffold

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