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Fig. 16 (a) Description of the detection of amyloid fibrils in proteins with an anionic conjugated
polymer, PTAA. (b) Emission spectra ( bottom ) of PTAA-Native bovine insulin ( filled square ) and
PTAA-amyloid fibrillar bovine insulin ( ). (c) Kinetics of insulin amyloid fibril formation
monitored by PTAA fluorescence [ 29 ]
solution had an absorption maximum of 446 nm, which was blue-shifted to 434 nm
upon addition of the bovine insulin monomer and then red-shifted again with the
formation of bovine insulin fibrils. The red-shift can again be associated with
planarization of the polymer backbone and extended conjugation upon interaction
with the
-sheet structure of the amyloid fibrils. A red shift was also seen for
the emission spectra for PTAA bound to insulin fibrils (Fig. 16 ). The emission
maximum was shifted from 550 to 580 nm and by plotting the ration of the emitted
b
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