Changing Times: Fluorescence-lifetime Analysis of Amyloidogenic SF-IAPP Fusion Protein
The fluorescence lifetime of the superfolder green fluorescent protein (SF) and the SF protein fused with islet amyloid polypeptide (SF-IAPP) were studied in polyacrylamide gel. It was shown that the SF average fluorescence lifetime under these conditions slightly differs from that of the SF-IAPP mo...
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Published in | bioRxiv |
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Main Authors | , , , , , |
Format | Paper |
Language | English |
Published |
Cold Spring Harbor
Cold Spring Harbor Laboratory Press
09.05.2018
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Subjects | |
Online Access | Get full text |
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Summary: | The fluorescence lifetime of the superfolder green fluorescent protein (SF) and the SF protein fused with islet amyloid polypeptide (SF-IAPP) were studied in polyacrylamide gel. It was shown that the SF average fluorescence lifetime under these conditions slightly differs from that of the SF-IAPP monomer. SF-IAPP does not lose the ability to form amyloid-like fibrils; meanwhile, the average fluorescence lifetime of the fusion protein in fibrils is reduced. We propose the application of Fluorescent-lifetime Imaging Microscopy (FLIM) to the measurement of average fluorescence lifetimes of fusion proteins (amyloidogenic protein-SF) in the context of studies using cellular models of conformational diseases. Footnotes * Misprint in abstract was corrected. |
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DOI: | 10.1101/317917 |