Lybatides from Lycium barbarum contain an unusual cystine-stapled helical peptide scaffold

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...

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Main Authors: Tan, Wei Liang, Wong, Ka Ho, Lei, Jian, Sakai, Naoki, Tan, Hong Wei, Hilgenfeld, Rolf, Tam, James P.
Other Authors: School of Biological Sciences
Format: Article
Language:English
Published: 2018
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Online Access:https://hdl.handle.net/10356/88139
http://hdl.handle.net/10220/45616
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Institution: Nanyang Technological University
Language: English
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spelling sg-ntu-dr.10356-881392023-02-28T16:56:34Z Lybatides from Lycium barbarum contain an unusual cystine-stapled helical peptide scaffold Tan, Wei Liang Wong, Ka Ho Lei, Jian Sakai, Naoki Tan, Hong Wei Hilgenfeld, Rolf Tam, James P. School of Biological Sciences Cysteine-rich Peptides Lybatide DRNTU::Science::Biological sciences 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. NRF (Natl Research Foundation, S’pore) Published version 2018-08-20T04:36:40Z 2019-12-06T16:56:55Z 2018-08-20T04:36:40Z 2019-12-06T16:56:55Z 2017 Journal Article Tan, W. L., Wong, K. H., Lei, J., Sakai, N., Tan, H. W., Hilgenfeld, R., & Tam, J. P. (2017). Lybatides from Lycium barbarum contain an unusual cystine-stapled helical peptide scaffold. Scientific Reports, 7, 5194-. doi:10.1038/s41598-017-05037-1 2045-2322 https://hdl.handle.net/10356/88139 http://hdl.handle.net/10220/45616 10.1038/s41598-017-05037-1 en Scientific Reports © 2017 The Author(s). This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. 11 p. application/pdf
institution Nanyang Technological University
building NTU Library
continent Asia
country Singapore
Singapore
content_provider NTU Library
collection DR-NTU
language English
topic Cysteine-rich Peptides
Lybatide
DRNTU::Science::Biological sciences
spellingShingle Cysteine-rich Peptides
Lybatide
DRNTU::Science::Biological sciences
Tan, Wei Liang
Wong, Ka Ho
Lei, Jian
Sakai, Naoki
Tan, Hong Wei
Hilgenfeld, Rolf
Tam, James P.
Lybatides from Lycium barbarum contain an unusual cystine-stapled helical peptide scaffold
description 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.
author2 School of Biological Sciences
author_facet School of Biological Sciences
Tan, Wei Liang
Wong, Ka Ho
Lei, Jian
Sakai, Naoki
Tan, Hong Wei
Hilgenfeld, Rolf
Tam, James P.
format Article
author Tan, Wei Liang
Wong, Ka Ho
Lei, Jian
Sakai, Naoki
Tan, Hong Wei
Hilgenfeld, Rolf
Tam, James P.
author_sort Tan, Wei Liang
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
publishDate 2018
url https://hdl.handle.net/10356/88139
http://hdl.handle.net/10220/45616
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