Okeudo-Cogan, M.C., Murray, B.S. orcid.org/0000-0002-6493-1547, Ettelaie, R. orcid.org/0000-0002-6970-4650 et al. (6 more authors) (2025) Unravelling Protein–Fungal Hyphae Interactions at the Nanoscale. ACS Applied Materials & Interfaces. ISSN 1944-8244
Abstract
Fungal hyphae have demonstrated their importance in developing environmentally friendly, multiscale, composite assemblies where animal-derived proteins have been predominantly used as binders. Now, an ongoing challenge is to replace those high-performance animal protein binders with ecofriendly, plant-based alternatives. While the majority of studies have focused on the binding implied by rheological observations, relatively little is known about how such animal proteins bind to hyphal surfaces at nanometric length scales, and this knowledge is required to replace animal-derived binders with plant protein alternatives. Here, we decode intermolecular interactions of plant protein-based binders such as potato protein (PoP) to fungal (Fusarium venenatum) hyphae in comparison to a classic animal protein-based binder (egg white protein, EWP) using a suite of theoretical and experimental approaches. Self-consistent field calculations modeling fungal hyphae as weakly hydrophobic, parallel cylinders predicted differences in the interaction potentials between the model protein layers, showing that EWP had an attractive potential across a broad range of conditions, in contrast to PoP that was mainly repulsive. Stimulated emission depletion (STED) microscopy of protein-coated fungal hyphae confirmed that EWP delivers a uniform and complete coverage, while PoP naturally aggregates, resulting in more patchy coverage. Experimental interaction forces were measured using colloidal probe atomic force microscopy, confirming the influence of non-Coulombic forces particularly dominating in PoP, and attractive forces in EWP, further differentiating their respective binding mechanisms. Collectively, this multimethodological study provides a first-hand molecular explanation of the weaker hyphal-binding properties of aggregated plant proteins at the nanoscale, consistent with the previously reported macroscale observations.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2025 The Authors. Published by American Chemical Society. This publication is licensed under CC-BY 4.0 . |
Keywords: | self-consistent field calculations; colloidal interactions; protein adsorption; meat analogues; DLVO; STED; AFM |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Environment (Leeds) > School of Food Science and Nutrition (Leeds) The University of Leeds > Faculty of Engineering & Physical Sciences (Leeds) > School of Physics and Astronomy (Leeds) The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) |
Funding Information: | Funder Grant number BBSRC (Biotechnology & Biological Sciences Research Council) BB/Z516119/1 |
Depositing User: | Symplectic Publications |
Date Deposited: | 24 Apr 2025 14:25 |
Last Modified: | 24 Apr 2025 14:25 |
Status: | Published online |
Publisher: | American Chemical Society (ACS) |
Identification Number: | 10.1021/acsami.5c01064 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:225631 |