Abstract
We report on the photophysical and optical properties of a polyfluorene derivative (PFO) and its binding to the amyloid-forming protein insulin.
Highlights
Conjugated polymers have attracted much attention as effective probes for amyloid protein bril recognition and are being developed for imaging, diagnostic and therapeutic applications[1]
The complexation is based on weak supramolecular interactions between amyloid fibrils and polyfluorene derivative (PFO) in dissolved and aggregated forms
We propose that a two-photon absorption enhancement mechanism is related to the combination of through-bond and through-space interactions of PFO
Summary
Conjugated polymers have attracted much attention as effective probes for amyloid protein bril recognition and are being developed for imaging, diagnostic and therapeutic applications[1]. Their tunable photophysical properties in the visible and near-infrared spectrum, which is sensitive to protein conformation upon binding, allow for monitoring of the brillization with a variety of optical techniques[2]. In order to use multiphoton based techniques molecules with large two-photon absorption cross-sections are required that enable efficient excitation in the near infrared region, which is safe for biomolecules. In case of the rst group the functional charged groups enhance the interaction with amyloids due to electrostatic binding with charged residues in the proto laments of the brils[5], whereas for the second group only weaker (stacking type) interaction occurs that is sensitive to small structural changes and the mode of interactions with the brils
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