Identification and characterization of a wolfberry carboxypeptidase inhibitor from Lycium barbarum

Hyperstable cysteine-rich peptides (CRPs) represent an underexplored superfamily of bioactives in functional foods. An example is wolfberry of the Lycium barbarum family. Previously, we discovered a CRP, designated α-lybatide, from L. barbarum bark. Herein, we report the discovery of β-lybatide, a n...

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Main Authors: Huang, Jiayi, Wong, Ka Ho, Tan, Wei Liang, Tay, Stephanie Victoria, Wang, Shujing, Tam, James P.
Other Authors: School of Biological Sciences
Format: Article
Language:English
Published: 2021
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Online Access:https://hdl.handle.net/10356/148027
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Institution: Nanyang Technological University
Language: English
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spelling sg-ntu-dr.10356-1480272023-02-28T17:09:09Z Identification and characterization of a wolfberry carboxypeptidase inhibitor from Lycium barbarum Huang, Jiayi Wong, Ka Ho Tan, Wei Liang Tay, Stephanie Victoria Wang, Shujing Tam, James P. School of Biological Sciences Science Carboxypeptidase Inhibitor Wolfberry Hyperstable cysteine-rich peptides (CRPs) represent an underexplored superfamily of bioactives in functional foods. An example is wolfberry of the Lycium barbarum family. Previously, we discovered a CRP, designated α-lybatide, from L. barbarum bark. Herein, we report the discovery of β-lybatide, a novel carboxypeptidase inhibitor belonging to a different CRP family from the wolfberry plant. Proteomic and transcriptomic analyses showed that β-lybatide contains 36 amino acids with six cysteine residues. NMR spectroscopy revealed that β-lybatide displays a knottin-like structure that renders it highly resistant to thermal, chemical and enzymatic degradation, conditions important for keeping its structural integrity in gastrointestinal tract. Biochemical assays showed that β-lybatide is a potent carboxypeptidase inhibitor which could contribute to the wolfberry biological activities. Bioinformatics analysis revealed an additional 49 β-lybatide-like plant carboxypeptidase inhibitors. Together, our results show that β-lybatide is the first and the smallest plant-derived hyperstable carboxypeptidase inhibitor discovered from a functional food. Ministry of Education (MOE) Accepted version This research was supported by a Nanyang Technological University internal funding – Synzymes and Natural Products (SYNC) and the AcRF Tier 3 funding (MOE2016-T3-1-003). 2021-04-22T08:03:29Z 2021-04-22T08:03:29Z 2021 Journal Article Huang, J., Wong, K. H., Tan, W. L., Tay, S. V., Wang, S. & Tam, J. P. (2021). Identification and characterization of a wolfberry carboxypeptidase inhibitor from Lycium barbarum. Food Chemistry, 351, 129338-. https://dx.doi.org/10.1016/j.foodchem.2021.129338 0308-8146 https://hdl.handle.net/10356/148027 10.1016/j.foodchem.2021.129338 33647700 2-s2.0-85101654830 351 129338 en MOE2016-T3-1-003 Synzymes and Natural Products Food Chemistry © 2021 Elsevier Ltd. All rights reserved. This paper was published in Food Chemistry and is made available with permission of Elsevier Ltd. application/pdf
institution Nanyang Technological University
building NTU Library
continent Asia
country Singapore
Singapore
content_provider NTU Library
collection DR-NTU
language English
topic Science
Carboxypeptidase Inhibitor
Wolfberry
spellingShingle Science
Carboxypeptidase Inhibitor
Wolfberry
Huang, Jiayi
Wong, Ka Ho
Tan, Wei Liang
Tay, Stephanie Victoria
Wang, Shujing
Tam, James P.
Identification and characterization of a wolfberry carboxypeptidase inhibitor from Lycium barbarum
description Hyperstable cysteine-rich peptides (CRPs) represent an underexplored superfamily of bioactives in functional foods. An example is wolfberry of the Lycium barbarum family. Previously, we discovered a CRP, designated α-lybatide, from L. barbarum bark. Herein, we report the discovery of β-lybatide, a novel carboxypeptidase inhibitor belonging to a different CRP family from the wolfberry plant. Proteomic and transcriptomic analyses showed that β-lybatide contains 36 amino acids with six cysteine residues. NMR spectroscopy revealed that β-lybatide displays a knottin-like structure that renders it highly resistant to thermal, chemical and enzymatic degradation, conditions important for keeping its structural integrity in gastrointestinal tract. Biochemical assays showed that β-lybatide is a potent carboxypeptidase inhibitor which could contribute to the wolfberry biological activities. Bioinformatics analysis revealed an additional 49 β-lybatide-like plant carboxypeptidase inhibitors. Together, our results show that β-lybatide is the first and the smallest plant-derived hyperstable carboxypeptidase inhibitor discovered from a functional food.
author2 School of Biological Sciences
author_facet School of Biological Sciences
Huang, Jiayi
Wong, Ka Ho
Tan, Wei Liang
Tay, Stephanie Victoria
Wang, Shujing
Tam, James P.
format Article
author Huang, Jiayi
Wong, Ka Ho
Tan, Wei Liang
Tay, Stephanie Victoria
Wang, Shujing
Tam, James P.
author_sort Huang, Jiayi
title Identification and characterization of a wolfberry carboxypeptidase inhibitor from Lycium barbarum
title_short Identification and characterization of a wolfberry carboxypeptidase inhibitor from Lycium barbarum
title_full Identification and characterization of a wolfberry carboxypeptidase inhibitor from Lycium barbarum
title_fullStr Identification and characterization of a wolfberry carboxypeptidase inhibitor from Lycium barbarum
title_full_unstemmed Identification and characterization of a wolfberry carboxypeptidase inhibitor from Lycium barbarum
title_sort identification and characterization of a wolfberry carboxypeptidase inhibitor from lycium barbarum
publishDate 2021
url https://hdl.handle.net/10356/148027
_version_ 1759857625077383168