Plant Natriuretic Peptide Active Domain Forms Amyloid-like Fibrils in a PH-Dependent Manner

Overview

Journal Plants (Basel)

Date 2022 Jan 11

PMID 35009013

Authors

Georgia I Nasi

Foteini D Aktypi

Panagiotis M Spatharas

Nikolaos N Louros

Paraskevi L Tsiolaki

Vassiliki Magafa

Ioannis P Trougakos

Vassiliki A Iconomidou

Affiliations

Soon will be listed here.

Abstract

Plant natriuretic peptides (PNPs) are hormones that have been extracted from many different species, with the 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 proteins. Our results reveal a new case of a pH-dependent amyloid forming peptide in , with a potential functional role.

Citing Articles

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Louros N, Schymkowitz J, Rousseau F Nat Rev Mol Cell Biol. 2023; 24(12):912-933.

PMID: 37684425 DOI: 10.1038/s41580-023-00647-2.

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