Dependence of the Nanoscale Composite Morphology of Fe<sub>3</sub>O<sub>4</sub> Nanoparticle-Infused Lysozyme Amyloid Fibrils on Timing of Infusion: A Combined SAXS and AFM Study
Understanding the formation process and the spatial distribution of nanoparticle (NP) clusters on amyloid fibrils is an essential step for the development of NP-based methods to inhibit aggregation of amyloidal proteins or reverse the assembling trend of the proto-fibrillary complexes that prompts p...
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MDPI AG
2021-08-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/26/16/4864 |
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| author | Martin A. Schroer Po-Sheng Hu Natalia Tomasovicova Marianna Batkova Katarina Zakutanska Po-Yi Wu Peter Kopcansky |
| author_facet | Martin A. Schroer Po-Sheng Hu Natalia Tomasovicova Marianna Batkova Katarina Zakutanska Po-Yi Wu Peter Kopcansky |
| author_sort | Martin A. Schroer |
| collection | DOAJ |
| description | Understanding the formation process and the spatial distribution of nanoparticle (NP) clusters on amyloid fibrils is an essential step for the development of NP-based methods to inhibit aggregation of amyloidal proteins or reverse the assembling trend of the proto-fibrillary complexes that prompts pathogenesis of neuro degeneration. For this, a detailed structural determination of the diverse hybrid assemblies that are forming is needed, which can be achieved by advanced X-ray scattering techniques. Using a combined solution small angle X-ray scattering (SAXS) and atomic force microscopy (AFM) approach, this study investigates the intrinsic trends of the interaction between lysozyme amyloid fibrils (LAFs) and Fe<sub>3</sub>O<sub>4</sub> NPs before and after fibrillization at nanometer resolution. AFM images reveal that the number of NP clusters interacting with the lysozyme fibers does not increase significantly with NP volume concentration, suggesting a saturation in NP aggregation on the fibrillary surface. The data indicate that the number of non-adsorbed Fe<sub>3</sub>O<sub>4</sub> NPs is highly dependent on the timing of NP infusion within the synthesis process. SAXS data yield access to the spatial distribution, aggregation manner and density of NP clusters on the fibrillary surfaces. Employing modern data analysis approaches, the shape and internal structural morphology of the so formed nanocomposites are revealed. The combined experimental approach suggests that while Fe<sub>3</sub>O<sub>4</sub> NPs infusion does not prevent the fibril-formation, the variation of NP concentration and size at different stages of the fibrillization process can impose a pronounced impact on the superficial and internal structural morphologies of these nanocomposites. These findings may be applicable in devising advanced therapeutic treatments for neurodegenerative diseases and designing novel bio-inorganic magnetic devices. Our results further demonstrate that modern X-ray methods give access to the structure of—and insight into the formation process of—biological–inorganic hybrid structures in solution. |
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| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-03-10T08:33:00Z |
| publishDate | 2021-08-01 |
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| series | Molecules |
| spelling | doaj.art-3983fadc48a84aca907c15fbd99ae8f32023-11-22T08:53:07ZengMDPI AGMolecules1420-30492021-08-012616486410.3390/molecules26164864Dependence of the Nanoscale Composite Morphology of Fe<sub>3</sub>O<sub>4</sub> Nanoparticle-Infused Lysozyme Amyloid Fibrils on Timing of Infusion: A Combined SAXS and AFM StudyMartin A. Schroer0Po-Sheng Hu1Natalia Tomasovicova2Marianna Batkova3Katarina Zakutanska4Po-Yi Wu5Peter Kopcansky6European Molecular Biology Laboratory, Hamburg Outstation c/o DESY, Notkestr. 85, 22607 Hamburg, GermanyCollege of Photonics, National Yang Ming Chiao Tung University, Tainan City 71150, TaiwanInstitute of Experimental Physics, Slovak Academy of Sciences, Watsonova 47, 04001 Kosice, SlovakiaInstitute of Experimental Physics, Slovak Academy of Sciences, Watsonova 47, 04001 Kosice, SlovakiaInstitute of Experimental Physics, Slovak Academy of Sciences, Watsonova 47, 04001 Kosice, SlovakiaCollege of Photonics, National Yang Ming Chiao Tung University, Tainan City 71150, TaiwanInstitute of Experimental Physics, Slovak Academy of Sciences, Watsonova 47, 04001 Kosice, SlovakiaUnderstanding the formation process and the spatial distribution of nanoparticle (NP) clusters on amyloid fibrils is an essential step for the development of NP-based methods to inhibit aggregation of amyloidal proteins or reverse the assembling trend of the proto-fibrillary complexes that prompts pathogenesis of neuro degeneration. For this, a detailed structural determination of the diverse hybrid assemblies that are forming is needed, which can be achieved by advanced X-ray scattering techniques. Using a combined solution small angle X-ray scattering (SAXS) and atomic force microscopy (AFM) approach, this study investigates the intrinsic trends of the interaction between lysozyme amyloid fibrils (LAFs) and Fe<sub>3</sub>O<sub>4</sub> NPs before and after fibrillization at nanometer resolution. AFM images reveal that the number of NP clusters interacting with the lysozyme fibers does not increase significantly with NP volume concentration, suggesting a saturation in NP aggregation on the fibrillary surface. The data indicate that the number of non-adsorbed Fe<sub>3</sub>O<sub>4</sub> NPs is highly dependent on the timing of NP infusion within the synthesis process. SAXS data yield access to the spatial distribution, aggregation manner and density of NP clusters on the fibrillary surfaces. Employing modern data analysis approaches, the shape and internal structural morphology of the so formed nanocomposites are revealed. The combined experimental approach suggests that while Fe<sub>3</sub>O<sub>4</sub> NPs infusion does not prevent the fibril-formation, the variation of NP concentration and size at different stages of the fibrillization process can impose a pronounced impact on the superficial and internal structural morphologies of these nanocomposites. These findings may be applicable in devising advanced therapeutic treatments for neurodegenerative diseases and designing novel bio-inorganic magnetic devices. Our results further demonstrate that modern X-ray methods give access to the structure of—and insight into the formation process of—biological–inorganic hybrid structures in solution.https://www.mdpi.com/1420-3049/26/16/4864nanocompositesbiological–nanoparticle hybrid systemslysozyme amyloid fibrilssmall angle X-ray scattering (SAXS)atomic force microscopy (AFM) |
| spellingShingle | Martin A. Schroer Po-Sheng Hu Natalia Tomasovicova Marianna Batkova Katarina Zakutanska Po-Yi Wu Peter Kopcansky Dependence of the Nanoscale Composite Morphology of Fe<sub>3</sub>O<sub>4</sub> Nanoparticle-Infused Lysozyme Amyloid Fibrils on Timing of Infusion: A Combined SAXS and AFM Study Molecules nanocomposites biological–nanoparticle hybrid systems lysozyme amyloid fibrils small angle X-ray scattering (SAXS) atomic force microscopy (AFM) |
| title | Dependence of the Nanoscale Composite Morphology of Fe<sub>3</sub>O<sub>4</sub> Nanoparticle-Infused Lysozyme Amyloid Fibrils on Timing of Infusion: A Combined SAXS and AFM Study |
| title_full | Dependence of the Nanoscale Composite Morphology of Fe<sub>3</sub>O<sub>4</sub> Nanoparticle-Infused Lysozyme Amyloid Fibrils on Timing of Infusion: A Combined SAXS and AFM Study |
| title_fullStr | Dependence of the Nanoscale Composite Morphology of Fe<sub>3</sub>O<sub>4</sub> Nanoparticle-Infused Lysozyme Amyloid Fibrils on Timing of Infusion: A Combined SAXS and AFM Study |
| title_full_unstemmed | Dependence of the Nanoscale Composite Morphology of Fe<sub>3</sub>O<sub>4</sub> Nanoparticle-Infused Lysozyme Amyloid Fibrils on Timing of Infusion: A Combined SAXS and AFM Study |
| title_short | Dependence of the Nanoscale Composite Morphology of Fe<sub>3</sub>O<sub>4</sub> Nanoparticle-Infused Lysozyme Amyloid Fibrils on Timing of Infusion: A Combined SAXS and AFM Study |
| title_sort | dependence of the nanoscale composite morphology of fe sub 3 sub o sub 4 sub nanoparticle infused lysozyme amyloid fibrils on timing of infusion a combined saxs and afm study |
| topic | nanocomposites biological–nanoparticle hybrid systems lysozyme amyloid fibrils small angle X-ray scattering (SAXS) atomic force microscopy (AFM) |
| url | https://www.mdpi.com/1420-3049/26/16/4864 |
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