Near-Wall Aggregation of Amyloidogenic Aβ 1-40 Peptide: Direct Observation by the FRET
The formation of amyloid fibrils is one of the variants of the self-organization of polypeptide chains. For the amyloid aggregation, the solution must be oversaturated with proteins. The interface of the liquid (solution) and solid (vessel walls) phases can trigger the adsorption of protein molecule...
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MDPI AG
2021-12-01
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Series: | Molecules |
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Online Access: | https://www.mdpi.com/1420-3049/26/24/7590 |
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author | Natalia Katina Alisa Mikhaylina Nelly Ilina Irina Eliseeva Vitalii Balobanov |
author_facet | Natalia Katina Alisa Mikhaylina Nelly Ilina Irina Eliseeva Vitalii Balobanov |
author_sort | Natalia Katina |
collection | DOAJ |
description | The formation of amyloid fibrils is one of the variants of the self-organization of polypeptide chains. For the amyloid aggregation, the solution must be oversaturated with proteins. The interface of the liquid (solution) and solid (vessel walls) phases can trigger the adsorption of protein molecules, and the resulting oversaturation can initiate conformational transitions in them. In any laboratory experiment, we cannot exclude the presence of surfaces such as the walls of vessels, cuvettes, etc. However, in many works devoted to the study of amyloid formation, this feature is not considered. In our work, we investigated the behavior of the Aβ 1-40 peptide at the water–glass, water–quartz, and water–plastic interface. We carried out a series of simple experiments and showed that the Aβ 1-40 peptide is actively adsorbed on these surfaces, which leads to a significant interaction and aggregation of peptides. This means that the interface can be the place where the first amyloid nucleus appears. We suggest that this effect may also be one of the reasons for the difficulty of reproducing kinetic data when studying the aggregation of the amyloid of the Aβ 1-40 peptide and other amyloidogenic proteins |
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issn | 1420-3049 |
language | English |
last_indexed | 2024-03-10T03:28:17Z |
publishDate | 2021-12-01 |
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series | Molecules |
spelling | doaj.art-6bb0fdd5d9214977a5fdadde3c905fc92023-11-23T09:46:24ZengMDPI AGMolecules1420-30492021-12-012624759010.3390/molecules26247590Near-Wall Aggregation of Amyloidogenic Aβ 1-40 Peptide: Direct Observation by the FRETNatalia Katina0Alisa Mikhaylina1Nelly Ilina2Irina Eliseeva3Vitalii Balobanov4Institute of Protein Research, Pushchino, 142290 Moscow, RussiaInstitute of Protein Research, Pushchino, 142290 Moscow, RussiaInstitute of Protein Research, Pushchino, 142290 Moscow, RussiaInstitute of Protein Research, Pushchino, 142290 Moscow, RussiaInstitute of Protein Research, Pushchino, 142290 Moscow, RussiaThe formation of amyloid fibrils is one of the variants of the self-organization of polypeptide chains. For the amyloid aggregation, the solution must be oversaturated with proteins. The interface of the liquid (solution) and solid (vessel walls) phases can trigger the adsorption of protein molecules, and the resulting oversaturation can initiate conformational transitions in them. In any laboratory experiment, we cannot exclude the presence of surfaces such as the walls of vessels, cuvettes, etc. However, in many works devoted to the study of amyloid formation, this feature is not considered. In our work, we investigated the behavior of the Aβ 1-40 peptide at the water–glass, water–quartz, and water–plastic interface. We carried out a series of simple experiments and showed that the Aβ 1-40 peptide is actively adsorbed on these surfaces, which leads to a significant interaction and aggregation of peptides. This means that the interface can be the place where the first amyloid nucleus appears. We suggest that this effect may also be one of the reasons for the difficulty of reproducing kinetic data when studying the aggregation of the amyloid of the Aβ 1-40 peptide and other amyloidogenic proteinshttps://www.mdpi.com/1420-3049/26/24/7590amyloidogenesisaggregationadsorptionAβ 1-40 peptideboundary of liquid phase |
spellingShingle | Natalia Katina Alisa Mikhaylina Nelly Ilina Irina Eliseeva Vitalii Balobanov Near-Wall Aggregation of Amyloidogenic Aβ 1-40 Peptide: Direct Observation by the FRET Molecules amyloidogenesis aggregation adsorption Aβ 1-40 peptide boundary of liquid phase |
title | Near-Wall Aggregation of Amyloidogenic Aβ 1-40 Peptide: Direct Observation by the FRET |
title_full | Near-Wall Aggregation of Amyloidogenic Aβ 1-40 Peptide: Direct Observation by the FRET |
title_fullStr | Near-Wall Aggregation of Amyloidogenic Aβ 1-40 Peptide: Direct Observation by the FRET |
title_full_unstemmed | Near-Wall Aggregation of Amyloidogenic Aβ 1-40 Peptide: Direct Observation by the FRET |
title_short | Near-Wall Aggregation of Amyloidogenic Aβ 1-40 Peptide: Direct Observation by the FRET |
title_sort | near wall aggregation of amyloidogenic aβ 1 40 peptide direct observation by the fret |
topic | amyloidogenesis aggregation adsorption Aβ 1-40 peptide boundary of liquid phase |
url | https://www.mdpi.com/1420-3049/26/24/7590 |
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