Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/146970
Title: Astratides : insulin-modulating, insecticidal, and antifungal cysteine-rich peptides from Astragalus membranaceus
Authors: Huang, Jiayi
Wong, Ka Ho
Tay, Stephanie Victoria
Serra, Aida
Sze, Siu Kuan
Tam, James P.
Keywords: Science::Biological sciences
Issue Date: 2019
Source: Huang, J., Wong, K. H., Tay, S. V., Serra, A., Sze, S. K. & Tam, J. P. (2019). Astratides : insulin-modulating, insecticidal, and antifungal cysteine-rich peptides from Astragalus membranaceus. Journal of Natural Products, 82(2), 194-204. https://dx.doi.org/10.1021/acs.jnatprod.8b00521
Project: NRF-CRP8-2011-05
MOE2016-T3-1- 003
Journal: Journal of Natural Products
Abstract: Astragalus membranaceus root, Huang Qi in Chinese, is a popular medicinal herb traditionally used to regulate blood glucose. Herein, the identification and characterization of two families of cysteine-rich peptides (CRPs), designated α- and β-astratides, from A. membranaceus roots are reported. Proteomic analysis showed that α-astratide aM1 and β-astratide bM1 belong to two distinct CRP families. The six-cysteine-containing and proline-rich α-astratide aM1 displayed high sequence identity to Pea Albumin 1 Subunit b (PA1b), while the eight-cysteine-containing β-astratide bM1 showed sequence similarity to plant defensins. An antifungal assay revealed that bM1 possessed potent antifungal activity. In contrast, aM1 showed a cytotoxic effect against insect Sf9 cells. More importantly, aM1 decreased insulin secretion in mouse pancreatic β cells, suggesting it could interfere in glucose homeostasis, which accounts for the adaptogenic property of A. membranaceus. Phylogenetic clustering analysis suggested that the proline-rich aM1 is a putative prolyl oligopeptidase inhibitor and belongs to a novel subfamily of PA1b-like peptides, while bM1 belongs to a new subfamily of plant defensins. Together, the study reveals that astratides are multifunctional CRPs in plants, which expand the existing library of PA1b-like peptides and plant defensins and further our understanding of their roles in host-defense system and leads as peptidyl therapeutics.
URI: https://hdl.handle.net/10356/146970
ISSN: 0163-3864
DOI: 10.1021/acs.jnatprod.8b00521
Schools: School of Biological Sciences 
Rights: © 2019 American Chemical Society and American Society of Pharmacognosy. All rights reserved.
Fulltext Permission: none
Fulltext Availability: No Fulltext
Appears in Collections:SBS Journal Articles

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