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.
MANNO M, CRAPARO EF, MARTORANA V, BULONE D, SAN BIAGIO PL (2006). KINETICS OF INSULIN AGGREGATION: DISENTANGLEMENT OF AMYLOID FIBRILLATION FROM LARGE-SIZE CLUSTER FORMATION. BIOPHYSICAL JOURNAL, 90(12), 4585-4591 [10.1529/biophysj.105.077636].
KINETICS OF INSULIN AGGREGATION: DISENTANGLEMENT OF AMYLOID FIBRILLATION FROM LARGE-SIZE CLUSTER FORMATION
CRAPARO EF;SAN BIAGIO PL
2006-01-01
Abstract
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.
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