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Molecular-level insights into the surface-induced assembly of Functional Bacterial Amyloid

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  • Thorbjørn Vincent Sønderby, University of the Chinese Academy of Sciences, Sino-Danish Centre
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  • Yimin Zou, CAS Center for Excellence in Nanoscience, National Center for Nanoscience and Technology, Beijing 100190, China
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  • Pengyu Wang, CAS Center for Excellence in Nanoscience, National Center for Nanoscience and Technology, Beijing 100190, China
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  • Chen Wang, CAS Center for Excellence in Nanoscience, National Center for Nanoscience and Technology, Beijing 100190, China
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  • Daniel Erik Otzen

Protein coating material is important in many technological fields. The interaction between carbon nanomaterial and protein is especially interesting since it makes the development of novel hybrid materials possible. Functional Bacterial Amyloid (FuBA) is promising as a coating material because of its desirable features such as well-defined molecular structure, robustness against harsh conditions, and easily engineerable functionality. Here, we report the systematic assembly of the functional amyloid protein, CsgA from Escherichia coli (E. coli) on graphite. We characterize the assemblies using Scanning Tunnelling Microscopy (STM) and show that CsgA forms assemblies according to systematic patterns, dictated by the graphite lattice. In addition, we show that graphite flakes induce the fibrillization of CsgA, in vitro, suggesting a surface-induced conformational change of CsgA facilitated by the graphite lattice. Using coarse-grained molecular dynamics simulations, we model the adhesion and lamellar formation of a CsgA-derived peptide and conclude that peptides are adsorbed both as monomers and smaller aggregates leading initially to unordered graphite-bound aggregates which are followed by rearrangement into lamellar structures. Finally, we show that CsgA-derived peptides can be immobilized in very systematic assemblies and their molecular orientation can be tuned using a small chaperone-like molecule. Our findings have implications for the development of FuBA-based biosensors, catalysts, and other technologies requiring well-defined protein assemblies on graphite.

Original languageEnglish
JournalBiophysical Journal
Volume121
Issue18
Pages (from-to)3422-3434
Number of pages13
ISSN0006-3495
DOIs
Publication statusPublished - Sep 2022

Bibliographical note

Copyright © 2022 Biophysical Society. Published by Elsevier Inc. All rights reserved.

    Research areas

  • Amyloid/chemistry, Amyloidogenic Proteins/metabolism, Escherichia coli Proteins/metabolism, Escherichia coli/metabolism, Graphite, Peptides/chemistry

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