Insights into Insulin Fibril Assembly at Physiological and Acidic pH and Related Amyloid Intrinsic Fluorescence
| Autor: | Ivana Sirangelo, Gaetano Irace, Clara Iannuzzi, Margherita Borriello, Marianna Portaccio |
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| Přispěvatelé: | Iannuzzi, Clara, Borriello, Margherita, Portaccio, Marianna, Irace, Gaetano, Sirangelo, Ivana |
| Jazyk: | angličtina |
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Circular dichroism Amyloid Protein Folding amyloid aggregation medicine.medical_treatment Infrared spectroscopy Fibril Catalysis Article lcsh:Chemistry Inorganic Chemistry 03 medical and health sciences Spectroscopy Fourier Transform Infrared medicine Humans Insulin Physical and Theoretical Chemistry protein misfolding lcsh:QH301-705.5 Molecular Biology Spectroscopy Chemistry Amyloidosis Circular Dichroism Organic Chemistry amyloid intrinsic fluorescence General Medicine Hydrogen-Ion Concentration medicine.disease Fluorescence Computer Science Applications Kinetics 030104 developmental biology lcsh:Biology (General) lcsh:QD1-999 Biochemistry Diabetes Mellitus Type 2 Protein folding |
| Zdroj: | International Journal of Molecular Sciences International Journal of Molecular Sciences; Volume 18; Issue 12; Pages: 2551 International Journal of Molecular Sciences, Vol 18, Iss 12, p 2551 (2017) |
| ISSN: | 1422-0067 |
| Popis: | Human insulin is a widely used model protein for the study of amyloid formation as both associated to insulin injection amyloidosis in type II diabetes and highly prone to form amyloid fibrils in vitro. In this study, we aim to gain new structural insights into insulin fibril formation under two different aggregating conditions at neutral and acidic pH, using a combination of fluorescence, circular dichroism, Fourier-transform infrared spectroscopy, and transmission electron miscroscopy. We reveal that fibrils formed at neutral pH are morphologically different from those obtained at lower pH. Moreover, differences in FTIR spectra were also detected. In addition, only insulin fibrils formed at neutral pH showed the characteristic blue-green fluorescence generally associated to amyloid fibrils. So far, the molecular origin of this fluorescence phenomenon has not been clarified and different hypotheses have been proposed. In this respect, our data provide experimental evidence that allow identifying the molecular origin of such intrinsic property. |
| Databáze: | OpenAIRE |
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