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

Aggregation kinetics of the Aβ1-40 peptide monitored by NMR

Chem Commun (Camb). 2018 Jul 14;54(55):7601-7604. doi: 10.1039/c8cc01710g. Epub 2018 May 16.

Authors

Giovanni Bellomo¹, Sara Bologna¹, Leonardo Gonnelli¹, Enrico Ravera², Marco Fragai², Moreno Lelli², Claudio Luchinat³

Affiliations

¹ Magnetic Resonance Center (CERM), University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, Italy. lelli@cerm.unifi.it luchinat@cerm.unifi.it.
² Magnetic Resonance Center (CERM), University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, Italy. lelli@cerm.unifi.it luchinat@cerm.unifi.it and Department of Chemistry "Ugo Schiff", University of Florence, Via della Lastruccia 3, 50019 Sesto Fiorentino, Italy.
³ Magnetic Resonance Center (CERM), University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, Italy. lelli@cerm.unifi.it luchinat@cerm.unifi.it and Department of Chemistry "Ugo Schiff", University of Florence, Via della Lastruccia 3, 50019 Sesto Fiorentino, Italy and Giotto Biotech S.R.L., Via Madonna del Piano 6, 50019 Sesto Fiorentino, Florence, Italy.

PMID: 29767190
DOI: 10.1039/c8cc01710g

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.

MeSH terms

Amyloid beta-Peptides / chemistry*
Benzothiazoles
Fluorescence
Kinetics
Magnetic Resonance Spectroscopy
Models, Chemical
Particle Size
Peptide Fragments / chemistry*
Protein Multimerization
Thiazoles / chemistry

Substances

Amyloid beta-Peptides
Benzothiazoles
Peptide Fragments
Thiazoles
amyloid beta-protein (1-40)
thioflavin T