Kinetics of insulin aggregation: disentanglement of amyloid fibrillation from large-size cluster formation.
Kinetics of human insulin aggregation has been studied at pH 1.6 and 60 degrees C, when amyloid fibrils are formed. We developed a novel approach based on the analysis of scattered light intensity distribution, which allows distinguishing between small and large size aggregates. By this method, we observed an exponential growth of fibrillar aggregates implying a heterogeneous aggregation mechanism. Also, the apparent lag time observed, correlated with the major increase of thioflavin T fluorescence, has been assigned to the onset of large size cluster formation.
Institute of Biophysics at Palermo, Italian National Research Council, Palermo, Italy.
Mauro
M
Manno
Emanuela Fabiola
EF
Craparo
Vincenzo
V
Martorana
Donatella
D
Bulone
Pier Luigi
PL
San Biagio
D000682:Amyloid / Q000737:chemistry* / Q000648:ultrastructure; D052160:Benzothiazoles; D003198:Computer Simulation; D006801:Humans; D007328:Insulin / Q000737:chemistry*; D007700:Kinetics; D008956:Models, Chemical; D008958:Models, Molecular; D046912:Multiprotein Complexes / Q000737:chemistry / Q000648:ultrastructure; D010316:Particle Size; D013844:Thiazoles / Q000737:chemistry*
D000682:Amyloid; D052160:Benzothiazoles; D007328:Insulin; D046912:Multiprotein Complexes; D013844:Thiazoles; C009462:thioflavin T