hIAPP promotes Aβ42 oligomerization and formation of large aggregates
hIAPP is highly amyloidogenic and can act as a seed for Aβ aggregation18. It is likely that Aβ and hIAPP cross-seeding would be dependent on their respective structural similarities and intermolecular interactions, but the underlying molecular mechanisms are poorly understood at present. To investigate cross-seeding interactions of Aβ42 and hIAPP, we initially assessed the aggregation of Aβ42, hIAPP and a non-amyloidogenic IAPP control (rat amylin, rIAPP) individually and in combinations using Thioflavin-T (ThT) assays (Fig. 1).
Aggregation kinetics of Aβ42-IAPP mixtures. (A) Individual aggregation kinetics of disaggregated Aβ42, hIAPP and rIAPP (20 µM) alongside TBS control assessed by Thioflavin-T (ThT) fluorescence over a 26 h period (mean ± SEM, n = 3, p < 0.001). (B) Aggregation…
