Hierarchical propagation of structural features in protein nanomaterials
Journal article, 2022
Natural high-performance materials have inspired the exploration of novel materials from protein building blocks. The ability of proteins to self-organize into amyloid-like nanofibrils has opened an avenue to new materials by hierarchical assembly processes. As the mechanisms by which proteins form nanofibrils are becoming clear, the challenge now is to understand how the nanofibrils can be designed to form larger structures with defined order. We here report the spontaneous and reproducible formation of ordered microstructure in solution cast films from whey protein nanofibrils. The structural features are directly connected to the nanostructure of the protein fibrils, which is itself determined by the molecular structure of the building blocks. Hence, a hierarchical assembly process ranging over more than six orders of magnitude in size is described. The fibril length distribution is found to be the main determinant of the microstructure and the assembly process originates in restricted capillary flow induced by the solvent evaporation. We demonstrate that the structural features can be switched on and off by controlling the length distribution or the evaporation rate without losing the functional properties of the protein nanofibrils.
Author
Ayaka Kamada
University of Cambridge
Royal Institute of Technology (KTH)
Anja Herneke
Swedish University of Agricultural Sciences (SLU)
Patricia Lopez-Sanchez
Chalmers, Biology and Biological Engineering, Food and Nutrition Science
Constantin Harder
Technical University of Munich
Deutsches Elektronen-Synchrotron (DESY)
Eirini Ornithopoulou
Royal Institute of Technology (KTH)
Qiong Wu
Royal Institute of Technology (KTH)
Xinfeng Wei
Royal Institute of Technology (KTH)
Matthias Schwartzkopf
Deutsches Elektronen-Synchrotron (DESY)
Peter Mueller-Buschbaum
Technical University of Munich
Roth
Deutsches Elektronen-Synchrotron (DESY)
Royal Institute of Technology (KTH)
Mikael S. Hedenqvist
Royal Institute of Technology (KTH)
Maud Langton
Swedish University of Agricultural Sciences (SLU)
Christofer Lendel
Royal Institute of Technology (KTH)
Nanoscale
2040-3364 (ISSN) 2040-3372 (eISSN)
Vol. 14 6 2502-2510Subject Categories
Physical Chemistry
Biochemistry and Molecular Biology
Biophysics
DOI
10.1039/d1nr05571b
PubMed
35103743