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• W4200508474 abstract "Plant natriuretic peptides (PNPs) are hormones that have been extracted from many different species, with the Arabidopsis thaliana PNP (AtPNP-A) being the most studied among them. AtPNP-A is a signaling molecule that consists of 130 residues and is secreted into the apoplast, under conditions of biotic or abiotic stress. AtPNP-A has distant sequence homology with human ANP, a protein that forms amyloid fibrils in vivo. In this work, we investigated the amyloidogenic properties of a 34-residue-long peptide, located within the AtPNP-A sequence, in three different pH conditions, using transmission electron microscopy, X-ray fiber diffraction, ATR FT-IR spectroscopy, Congo red and Thioflavin T staining assays. We also utilize bioinformatics tools to study its association with known plant amyloidogenic proteins and other A. thaliana proteins. Our results reveal a new case of a pH-dependent amyloid forming peptide in A. thaliana, with a potential functional role." @default.
• W4200508474 created "2021-12-31" @default.
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• W4200508474 date "2021-12-21" @default.
• W4200508474 modified "2023-10-02" @default.
• W4200508474 title "Arabidopsis thaliana Plant Natriuretic Peptide Active Domain Forms Amyloid-like Fibrils in a pH-Dependent Manner" @default.
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• W4200508474 doi "https://doi.org/10.3390/plants11010009" @default.
• W4200508474 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/35009013" @default.
• W4200508474 hasPublicationYear "2021" @default.
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