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β-Ginkgotides: Hyperdisulfide-constrained peptides from Ginkgo biloba
Ka H Wong1, Wei Liang Tan1, Tianshu Xiao1
1School of Biological Sciences, Nanyang Technological University, Singapore, 637551, Singapore.
Scientific Reports
|July 23, 2017
Summary
Researchers discovered beta-ginkgotides, a novel family of stable, hyperdisulfide-constrained peptides in Ginkgo biloba. These plant-derived peptides possess a unique structure and resistance to degradation, offering potential for therapeutic applications.
Area of Science:
- Biochemistry
- Molecular Biology
- Phylogenetics
Background:
- Hyperdisulfide-constrained peptides are known for stability and function, predominantly found in animals.
- Their presence in plants is rare, limiting understanding of their evolutionary and functional diversity.
Purpose of the Study:
- To discover, synthesize, and characterize a novel family of hyperdisulfide-constrained peptides from Ginkgo biloba.
- To elucidate the unique structural features, disulfide connectivity, and evolutionary origins of these peptides.
Main Methods:
- Proteomic and transcriptomic analyses were employed to identify and characterize beta-ginkgotides and their precursors.
- Peptide synthesis, oxidative folding, NMR spectroscopy, and disulfide mapping were used to determine structure and connectivity.
- Phylogenetic analysis was conducted to understand the evolutionary placement of beta-ginkgotides.
Main Results:
- Discovery of beta-ginkgotides (β-gB1, β-gB2), approximately 2 kDa peptides from Ginkgo biloba.
- Identification of a conserved six-cysteine core with a novel clustered spacing (C‒CC‒C‒CC) and disulfide connectivity (CysI‒IV, CysII‒VI, CysIII‒V).
- Successful synthesis and oxidative folding of β-gB1, revealing a compact structure without regular secondary elements; identification of 76 related peptides in gymnosperms.
Conclusions:
- Beta-ginkgotides represent the first plant-derived hyperdisulfide-constrained peptide family with a novel scaffold.
- Their remarkable stability against thermal, chemical, and proteolytic degradation suggests potential for engineering metabolically stable peptidyl therapeutics.
- The findings expand the known diversity of cysteine-rich peptides and their evolutionary distribution.
