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Effect of the concentration of protein and nanoparticles on the structure of biohybrid nanocomposites
Author(s) -
Majorošová Jozefína,
Schroer Martin A.,
Tomašovičová Natália,
Batková Marianna,
Hu PoSheng,
Kubovčíková Martina,
Svergun Dmitri I.,
Kopčanský Peter
Publication year - 2020
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.23342
Subject(s) - nanocomposite , chemistry , chemical engineering , lysozyme , nanoparticle , dynamic light scattering , salt (chemistry) , morphology (biology) , colloid , glial fibrillary acidic protein , small angle x ray scattering , adsorption , biophysics , scattering , organic chemistry , biochemistry , medicine , physics , immunohistochemistry , optics , biology , engineering , genetics
We present colloidal nanocomposites formed by incorporating magnetite Fe 3 O 4 nanoparticles (MNPs) with lysozyme amyloid fibrils (LAFs). Preparation of two types of solutions, with and without addition of salt, was carried out to elucidate the structure of MNPs‐incorporated fibrillary nanocomposites and to study the effect of the presence of salt on the stability of the nanocomposites. The structural morphology of the LAFs and their interaction with MNPs were analyzed by atomic force microscopy and small‐angle x‐ray scattering measurements. The results indicate that conformational properties of the fibrils are dependent on the concentration of protein, and the precise ratio of the concentration of the protein and MNPs is crucially important for the stability of the fibrillary nanocomposites. Our results confirm that despite the change in fibrillary morphology induced by the varying concentration of the protein, the adsorption of MNPs on the surface of LAF is morphologically independent. Moreover, most importantly, the samples containing salt have excellent stability for up to 1 year of shelf‐life.