The Amyloid Fibril-Forming Properties of the Amphibian Antimicrobial Peptide Uperin 3.5

Antonio N Calabrese; Yanqin Liu; Tianfang Wang; Ian F Musgrave; Tara L Pukala; Rico F Tabor; Lisandra L Martin; John A Carver; John H Bowie

doi:10.1002/cbic.201500518

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The Amyloid Fibril-Forming Properties of the Amphibian Antimicrobial Peptide Uperin 3.5

Journal article

Peer reviewed

The Amyloid Fibril-Forming Properties of the Amphibian Antimicrobial Peptide Uperin 3.5

Antonio N Calabrese, Yanqin Liu, Tianfang Wang, Ian F Musgrave, Tara L Pukala, Rico F Tabor, Lisandra L Martin, John A Carver and John H Bowie

ChemBioChem, Vol.17(3), pp.239-246

2016

DOI: https://doi.org/10.1002/cbic.201500518

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Abstract

aggregation

amyloid

antimicrobial peptides

mass spectrometry

uperin

The amphibian skin is a vast resource for bioactive peptides, which form the basis of the animals' innate immune system. Key components of the secretions of the cutaneous glands are antimicrobial peptides (AMPs), which exert their cytotoxic effects often as a result of membrane disruption. It is becoming increasingly evident that there is a link between the mechanism of action of AMPs and amyloidogenic peptides and proteins. In this work, we demonstrate that the broad-spectrum amphibian AMP uperin 3.5, which has a random-coil structure in solution but adopts an α-helical structure in membrane-like environments, forms amyloid fibrils rapidly in solution at neutral pH. These fibrils are cytotoxic to model neuronal cells in a similar fashion to those formed by the proteins implicated in neurodegenerative diseases. The addition of small quantities of 2,2,2-trifluoroethanol accelerates fibril formation by uperin 3.5, and is correlated with a structural stabilisation induced by this co-solvent. Uperin 3.5 fibril formation and the associated cellular toxicity are inhibited by the polyphenol (-)-epigallocatechin-3-gallate (EGCG). Furthermore, EGCG rapidly dissociates fully formed uperin 3.5 fibrils. Ion mobility-mass spectrometry reveals that uperin 3.5 adopts various oligomeric states in solution. Combined, these observations imply that the mechanism of membrane permeability by uperin 3.5 is related to its fibril-forming properties.

Details

Title: The Amyloid Fibril-Forming Properties of the Amphibian Antimicrobial Peptide Uperin 3.5
Authors: Antonio N Calabrese (Author) - University of Adelaide
Yanqin Liu (Author) - University of Adelaide
Tianfang Wang (Author) - University of the Sunshine Coast - Faculty of Science, Health, Education and Engineering
Ian F Musgrave (Author) - University of Adelaide
Tara L Pukala (Author) - University of Adelaide
Rico F Tabor (Author) - Monash University
Lisandra L Martin (Author) - Monash University
John A Carver (Author) - Australian National University
John H Bowie (Author) - University of Adelaide
Publication details: ChemBioChem, Vol.17(3), pp.239-246
Publisher: Wiley - V C H Verlag GmbH & Co. KGaA
Date published: 2016
DOI: 10.1002/cbic.201500518
ISSN: 1439-4227
Organisation Unit: School of Science and Engineering - Legacy; University of the Sunshine Coast, Queensland; School of Science, Technology and Engineering; Centre for Bioinnovation
Language: English
Record Identifier: 99449281502621
Output Type: Journal article

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Collaboration types: Domestic collaboration; International collaboration
Web Of Science research areas: Biochemistry & Molecular Biology; Chemistry, Medicinal

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