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...

Full description

Bibliographic Details
Main Authors: Natalia Katina, Alisa Mikhaylina, Nelly Ilina, Irina Eliseeva, Vitalii Balobanov
Format: Article
Language:English
Published: MDPI AG 2021-12-01
Series:Molecules
Subjects:
Online Access:https://www.mdpi.com/1420-3049/26/24/7590
_version_ 1797502115228155904
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
first_indexed 2024-03-10T03:28:17Z
format Article
id doaj.art-6bb0fdd5d9214977a5fdadde3c905fc9
institution Directory Open Access Journal
issn 1420-3049
language English
last_indexed 2024-03-10T03:28:17Z
publishDate 2021-12-01
publisher MDPI AG
record_format Article
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
work_keys_str_mv AT nataliakatina nearwallaggregationofamyloidogenicab140peptidedirectobservationbythefret
AT alisamikhaylina nearwallaggregationofamyloidogenicab140peptidedirectobservationbythefret
AT nellyilina nearwallaggregationofamyloidogenicab140peptidedirectobservationbythefret
AT irinaeliseeva nearwallaggregationofamyloidogenicab140peptidedirectobservationbythefret
AT vitaliibalobanov nearwallaggregationofamyloidogenicab140peptidedirectobservationbythefret