β-Ginkgotides: Hyperdisulfide-constrained peptides from Ginkgo biloba
Hyperdisulfide-constrained peptides are distinguished by their high stability and diverse functions. Thus far, these peptides have been reported from animals only but their occurrence in plants are rare. Here, we report the discovery, synthesis and characterization of a hyperdisulfide-constrained pe...
| Main Authors: | , , , |
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| Format: | Journal Article |
| Language: | English |
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2017
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| Online Access: | https://hdl.handle.net/10356/86680 http://hdl.handle.net/10220/44121 |
| _version_ | 1824457152681476096 |
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| author | Wong, Ka Ho Tan, Wei Liang Xiao, Tianshu Tam, James P. |
| author2 | School of Biological Sciences |
| author_facet | School of Biological Sciences Wong, Ka Ho Tan, Wei Liang Xiao, Tianshu Tam, James P. |
| author_sort | Wong, Ka Ho |
| collection | NTU |
| description | Hyperdisulfide-constrained peptides are distinguished by their high stability and diverse functions. Thus far, these peptides have been reported from animals only but their occurrence in plants are rare. Here, we report the discovery, synthesis and characterization of a hyperdisulfide-constrained peptides family of approximately 2 kDa, β-ginkgotides (β-gB1 and β-gB2) from Ginkgo biloba. Proteomic analysis showed β-ginkgotides contain 18‒20 amino acids, of which 16 residues form a conserved six-cysteine core with a highly clustered cysteine spacing of C‒CC‒C‒CC, an arrangement that has not been reported in cysteine-rich peptides. Disulfide mapping revealed a novel disulfide connectivity of CysI‒IV, CysII‒VI and CysIII‒V. Oxidative folding of synthetic β-gB1 to the native form was obtained in 70% yield. The synthetic β-gB1 displays a compact structure with no regular secondary structural elements, as determined by NMR spectroscopy. Transcriptomic analysis showed precursor βgb1 has a four-domain architecture and revealed an additional 76 β-ginkgotide-like peptides in 59 different gymnosperms, but none in angiosperms. Phylogenetic clustering analysis demonstrated β-ginkgotides belong to a new cysteine-rich peptide family. β-Ginkgotide is resistant to thermal, chemical and proteolytic degradation. Together, β-ginkgotides represent the first-in-class hyperdisulfide-constrained peptide family from plants with a novel scaffold that could be useful for engineering metabolically stable peptidyl therapeutics. |
| first_indexed | 2025-02-19T04:05:27Z |
| format | Journal Article |
| id | ntu-10356/86680 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2025-02-19T04:05:27Z |
| publishDate | 2017 |
| record_format | dspace |
| spelling | ntu-10356/866802023-02-28T17:01:44Z β-Ginkgotides: Hyperdisulfide-constrained peptides from Ginkgo biloba Wong, Ka Ho Tan, Wei Liang Xiao, Tianshu Tam, James P. School of Biological Sciences β-Ginkgotides Peptides Hyperdisulfide-constrained peptides are distinguished by their high stability and diverse functions. Thus far, these peptides have been reported from animals only but their occurrence in plants are rare. Here, we report the discovery, synthesis and characterization of a hyperdisulfide-constrained peptides family of approximately 2 kDa, β-ginkgotides (β-gB1 and β-gB2) from Ginkgo biloba. Proteomic analysis showed β-ginkgotides contain 18‒20 amino acids, of which 16 residues form a conserved six-cysteine core with a highly clustered cysteine spacing of C‒CC‒C‒CC, an arrangement that has not been reported in cysteine-rich peptides. Disulfide mapping revealed a novel disulfide connectivity of CysI‒IV, CysII‒VI and CysIII‒V. Oxidative folding of synthetic β-gB1 to the native form was obtained in 70% yield. The synthetic β-gB1 displays a compact structure with no regular secondary structural elements, as determined by NMR spectroscopy. Transcriptomic analysis showed precursor βgb1 has a four-domain architecture and revealed an additional 76 β-ginkgotide-like peptides in 59 different gymnosperms, but none in angiosperms. Phylogenetic clustering analysis demonstrated β-ginkgotides belong to a new cysteine-rich peptide family. β-Ginkgotide is resistant to thermal, chemical and proteolytic degradation. Together, β-ginkgotides represent the first-in-class hyperdisulfide-constrained peptide family from plants with a novel scaffold that could be useful for engineering metabolically stable peptidyl therapeutics. NRF (Natl Research Foundation, S’pore) Published version 2017-12-12T04:13:36Z 2019-12-06T16:27:11Z 2017-12-12T04:13:36Z 2019-12-06T16:27:11Z 2017 Journal Article Wong, K. H., Tan, W. L., Xiao, T., & Tam, J. P. (2017). β-Ginkgotides: Hyperdisulfide-constrained peptides from Ginkgo biloba. Scientific Reports, 7, 6140-. 2045-2322 https://hdl.handle.net/10356/86680 http://hdl.handle.net/10220/44121 10.1038/s41598-017-06598-x en Scientific Reports © 2017 The Author(s) (Nature Publishing Group). This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ 13 p. application/pdf |
| spellingShingle | β-Ginkgotides Peptides Wong, Ka Ho Tan, Wei Liang Xiao, Tianshu Tam, James P. β-Ginkgotides: Hyperdisulfide-constrained peptides from Ginkgo biloba |
| title | β-Ginkgotides: Hyperdisulfide-constrained peptides from Ginkgo biloba |
| title_full | β-Ginkgotides: Hyperdisulfide-constrained peptides from Ginkgo biloba |
| title_fullStr | β-Ginkgotides: Hyperdisulfide-constrained peptides from Ginkgo biloba |
| title_full_unstemmed | β-Ginkgotides: Hyperdisulfide-constrained peptides from Ginkgo biloba |
| title_short | β-Ginkgotides: Hyperdisulfide-constrained peptides from Ginkgo biloba |
| title_sort | β ginkgotides hyperdisulfide constrained peptides from ginkgo biloba |
| topic | β-Ginkgotides Peptides |
| url | https://hdl.handle.net/10356/86680 http://hdl.handle.net/10220/44121 |
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