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.
Aggregation kinetics of the Aβ1-40 peptide monitored by NMR / Bellomo G, Bologna S, Gonnelli L, Ravera E, Fragai M, Lelli M, Luchinat C. - In: CHEMICAL COMMUNICATIONS. - ISSN 1359-7345. - STAMPA. - 54:(2018), pp. 7601-7604. [10.1039/c8cc01710g]
Aggregation kinetics of the Aβ1-40 peptide monitored by NMR
BELLOMO, GIOVANNI;BOLOGNA, SARA;Gonnelli L;Ravera E;Fragai M;Lelli M
Supervision
;Luchinat C
2018
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.
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