Aggregation kinetics of the Aβ1–40 peptide monitored by NMR

Giovanni Bellomo; Sara Bologna; Leonardo Gonnelli; Enrico Ravera; Marco Fragai; Moreno Lelli; Claudio Luchinat

doi:10.1039/C8CC01710G

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Aggregation kinetics of the Aβ1–40 peptide monitored by NMR†

Giovanni Bellomo,

^a Sara Bologna,^a Leonardo Gonnelli,^a Enrico Ravera,

^ab Marco Fragai,

^ab Moreno Lelli

*^ab and Claudio Luchinat

*^abc

Author affiliations

* Corresponding authors

^a Magnetic Resonance Center (CERM), University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, Italy
E-mail: lelli@cerm.unifi.it, luchinat@cerm.unifi.it

^b Department of Chemistry “Ugo Schiff”, University of Florence, Via della Lastruccia 3, 50019 Sesto Fiorentino, Italy

^c Giotto Biotech S.R.L., Via Madonna del Piano 6, 50019 Sesto Fiorentino, Florence, Italy

Abstract

The aggregation of Aβ1–40 was monitored by solution NMR, which showed a trend complementary to the one observed by ThT-fluorescence. The NMR data support a kinetic model where Aβ1–40 initially aggregates with the reversible formation of oligomeric species, which then irreversibly convert into fibrils.

This article is part of the themed collection: Amyloid Aggregation

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Article information

DOI: https://doi.org/10.1039/C8CC01710G
Article type: Communication
Submitted: 20 Mar 2018
Accepted: 03 May 2018
First published: 16 May 2018

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Chem. Commun., 2018,54, 7601-7604

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Aggregation kinetics of the Aβ1–40 peptide monitored by NMR

G. Bellomo, S. Bologna, L. Gonnelli, E. Ravera, M. Fragai, M. Lelli and C. Luchinat, Chem. Commun., 2018, 54, 7601 DOI: 10.1039/C8CC01710G

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Chemical Communications

Aggregation kinetics of the Aβ1–40 peptide monitored by NMR†

Abstract

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Aggregation kinetics of the Aβ1–40 peptide monitored by NMR

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