β-Ginkgotides: Hyperdisulfide-constrained peptides from Ginkgo biloba

Abstract 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-const...

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Autores principales:	Ka H. Wong, Wei Liang Tan, Tianshu Xiao, James P. Tam
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/c505011489b84c82a6c69fadbb542779
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spelling	oai:doaj.org-article:c505011489b84c82a6c69fadbb5427792021-12-02T11:40:30Zβ-Ginkgotides: Hyperdisulfide-constrained peptides from Ginkgo biloba10.1038/s41598-017-06598-x2045-2322https://doaj.org/article/c505011489b84c82a6c69fadbb5427792017-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-06598-xhttps://doaj.org/toc/2045-2322Abstract 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.Ka H. WongWei Liang TanTianshu XiaoJames P. TamNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-13 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Ka H. Wong Wei Liang Tan Tianshu Xiao James P. Tam β-Ginkgotides: Hyperdisulfide-constrained peptides from Ginkgo biloba
description	Abstract 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.
format	article
author	Ka H. Wong Wei Liang Tan Tianshu Xiao James P. Tam
author_facet	Ka H. Wong Wei Liang Tan Tianshu Xiao James P. Tam
author_sort	Ka H. Wong
title	β-Ginkgotides: Hyperdisulfide-constrained peptides from Ginkgo biloba
title_short	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_sort	β-ginkgotides: hyperdisulfide-constrained peptides from ginkgo biloba
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/c505011489b84c82a6c69fadbb542779
work_keys_str_mv	AT kahwong bginkgotideshyperdisulfideconstrainedpeptidesfromginkgobiloba AT weiliangtan bginkgotideshyperdisulfideconstrainedpeptidesfromginkgobiloba AT tianshuxiao bginkgotideshyperdisulfideconstrainedpeptidesfromginkgobiloba AT jamesptam bginkgotideshyperdisulfideconstrainedpeptidesfromginkgobiloba
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β-Ginkgotides: Hyperdisulfide-constrained peptides from Ginkgo biloba

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