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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2017-07-01
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doaj-6bf374fb01a84458acc00e754ce89c4c2020-12-08T01:29:42ZengNature Publishing GroupScientific Reports2045-23222017-07-017111110.1038/s41598-017-05037-1Lybatides from Lycium barbarum Contain An Unusual Cystine-stapled Helical Peptide ScaffoldWei Liang Tan0Ka H. Wong1Jian Lei2Naoki Sakai3Hong Wei Tan4Rolf Hilgenfeld5James P. Tam6School of Biological Sciences, Nanyang Technological UniversitySchool of Biological Sciences, Nanyang Technological UniversityInstitute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of LübeckInstitute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of LübeckSchool of Biological Sciences, Nanyang Technological UniversityInstitute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of LübeckSchool of Biological Sciences, Nanyang Technological UniversityAbstract 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.https://doi.org/10.1038/s41598-017-05037-1 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Wei Liang Tan Ka H. Wong Jian Lei Naoki Sakai Hong Wei Tan Rolf Hilgenfeld James P. Tam |
spellingShingle |
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 Scientific Reports |
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 Publishing Group |
series |
Scientific Reports |
issn |
2045-2322 |
publishDate |
2017-07-01 |
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. |
url |
https://doi.org/10.1038/s41598-017-05037-1 |
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