CHANGES IN THE SECONDARY STRUCTURE AND ASSEMBLY OF PROTEINS ON FLUORIDE CERAMIC (CEF3) NANOPARTICLE SURFACES
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Date
2022
Authors
Sakaguchi, Naoya
Kaumbekova, Samal
Itano, Ryodai
Torkmahalleh, Mehdi Amouei
Shah, Dhawal
Umezawa, Masakazu
Journal Title
Journal ISSN
Volume Title
Publisher
ACS Applied Bio Materials
Abstract
Fluoride nanoparticles (NPs) are materials utilized in the biomedical
field for applications including imaging of the brain. Their interactions with biological
systems and molecules are being investigated, but the mechanism underlying these
interactions remains unclear. We focused on possible changes in the secondary structure
and aggregation state of proteins on the surface of NPs and investigated the principle
underlying the changes using the amyloid β peptide (Aβ16−20) based on infrared
spectrometry. CeF3 NPs (diameter 80 nm) were synthesized via thermal decomposition.
Infrared spectrometry showed that the presence of CeF3 NPs promotes the formation of
the β-sheet structure of Aβ16−20. This phenomenon was attributed to the hydrophobic
interaction between NPs and Aβ peptides in aqueous environments, which causes the Aβ peptides to approach each other on the NP
surface and form ordered hydrogen bonds. Because of the coexisting salts on the secondary structure and assembly of Aβ peptides,
the formation of the β-sheet structure of Aβ peptides on the NP surface was suppressed in the presence of NH4
+ and NO3
− ions,
suggesting the possibility that Aβ peptides were adsorbed and bound to the NP surface. The formation of the β-sheet structure of Aβ
peptides was promoted in the presence of NH4
+
, whereas it was suppressed in the presence of NO3
− because of the electrostatic
interaction between the lysine residue of the Aβ peptide and the ions. Our findings will contribute to comparative studies on the
effect of different NPs with different physicochemical properties on the molecular state of proteins.
Description
Keywords
Type of access: Open Access, amyloid β peptide, fluoride nanoparticles, infrared spectrometry, molecular dynamics, β-sheet
Citation
Sakaguchi, N., Kaumbekova, S., Itano, R., Torkmahalleh, M. A., Shah, D., & Umezawa, M. (2022). Changes in the Secondary Structure and Assembly of Proteins on Fluoride Ceramic (CeF3) Nanoparticle Surfaces. ACS Applied Bio Materials. https://doi.org/10.1021/acsabm.2c00239