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RESEARCH PRODUCT
Kinetics of Insulin Aggregation: Disentanglement of Amyloid Fibrillation from Large-Size Cluster Formation
Mauro MannoDonatella BulonePier Luigi San BiagioVincenzo MartoranaEmanuela Fabiola Craparosubject
MECHANISMModels MolecularAmyloidAmyloidmedicine.medical_treatmentKineticsBiophysicschemistry.chemical_compoundExponential growthFIBRILSmedicineCluster (physics)HumansInsulinComputer SimulationBenzothiazolesParticle SizeATOMIC-FORCE MICROSCOPYInsulinPATHWAYSProteinsFluorescenceLIGHT-SCATTERINGCrystallographyKineticsThiazoleschemistryModels ChemicalMultiprotein ComplexesBiophysicsThioflavinParticle sizeBETA-PROTEINNUCLEATIONdescription
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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2006-06-01 | Biophysical Journal |