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Michler's hydrol blue: a sensitive probe for amyloid fibril detection.

Abstract：

:Michler's hydrol blue (MHB) is investigated with respect to photophysical properties in varied solvent environment and when bound to insulin and lysozyme fibrils. The MHB chromophore is shown to act like a molecular rotor and bind well to amyloid fibrils, where it exhibits a characteristic red-shift in its excitation spectrum and an increase in the emission quantum yield upon binding. MHB is more sensitive to environmental changes than Thioflavin T (ThT) and furthermore, in contrast to the latter amyloid probe, can differentiate between insulin and lysozyme fibrils by a more red-shifted excitation spectrum for insulin fibrils. To support the experimental observations, time-dependent density functional theory (TDDFT) calculations were performed on MHB at several levels of theory. The predicted changes of spectral properties as a function of the environment are in good agreement with the experimental results. Linear dichroism (LD) is used to determine the orientation of the MHB within the fibrils. It was shown through LD and molecular modeling that MHB aligns itself preferentially parallel with the amyloid fiber at an angle of 14°-22° to the fibril axis and along the grooves of the β-sheet.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Kitts CC,Beke-Somfai T,Nordén B

doi

10.1021/bi102016p

subject

Has Abstract

pub_date

2011-05-03 00:00:00

pages

3451-61

issue

17

eissn

0006-2960

issn

1520-4995

journal_volume

50

pub_type

杂志文章

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