Hierarchical propagation of structural features in protein nanomaterials
Artikel i vetenskaplig tidskrift, 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.

Författare

Ayaka Kamada

University of Cambridge

Kungliga Tekniska Högskolan (KTH)

Anja Herneke

Sveriges lantbruksuniversitet (SLU)

Patricia Lopez-Sanchez

Chalmers, Biologi och bioteknik, Livsmedelsvetenskap

Constantin Harder

Technische Universität München

Deutsches Elektronen-Synchrotron (DESY)

Eirini Ornithopoulou

Kungliga Tekniska Högskolan (KTH)

Qiong Wu

Kungliga Tekniska Högskolan (KTH)

Xinfeng Wei

Kungliga Tekniska Högskolan (KTH)

Matthias Schwartzkopf

Deutsches Elektronen-Synchrotron (DESY)

Peter Mueller-Buschbaum

Technische Universität München

Roth

Deutsches Elektronen-Synchrotron (DESY)

Kungliga Tekniska Högskolan (KTH)

Mikael S. Hedenqvist

Kungliga Tekniska Högskolan (KTH)

Maud Langton

Sveriges lantbruksuniversitet (SLU)

Christofer Lendel

Kungliga Tekniska Högskolan (KTH)

Nanoscale

2040-3364 (ISSN) 2040-3372 (eISSN)

Vol. 14 6 2502-2510

Ämneskategorier

Fysikalisk kemi

Biokemi och molekylärbiologi

Biofysik

DOI

10.1039/d1nr05571b

PubMed

35103743

Mer information

Senast uppdaterat

2022-04-05