Please use this identifier to cite or link to this item:
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.
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.
ISSN: 0163-3864
DOI: 10.1021/acs.jnatprod.8b00521
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

Citations 20

Updated on Mar 28, 2023

Web of ScienceTM
Citations 20

Updated on Mar 22, 2023

Page view(s)

Updated on Mar 29, 2023

Google ScholarTM




Items in DR-NTU are protected by copyright, with all rights reserved, unless otherwise indicated.