Please use this identifier to cite or link to this item: https://doi.org/10.1021/jp906433u
Title: Fluorescence turn-on responses of anionic and cationic conjugated polymers toward proteins: Effect of electrostatic and hydrophobic interactions
Authors: Pu, K.-Y. 
Liu, B. 
Issue Date: 11-Mar-2010
Source: Pu, K.-Y., Liu, B. (2010-03-11). Fluorescence turn-on responses of anionic and cationic conjugated polymers toward proteins: Effect of electrostatic and hydrophobic interactions. Journal of Physical Chemistry B 114 (9) : 3077-3084. ScholarBank@NUS Repository. https://doi.org/10.1021/jp906433u
Abstract: Cationic and anionic poly(fluorenyleneethynylene-alt-benzothiadiazole)s (PFEBTs) are designed and synthesized via Sonagashira coupling reaction to show light-up signatures toward proteins. Due to the charge transfer character of the excited states, the fluorescence of PFEBTs is very weak in aqueous solution, while their yellow fluorescence can be enhanced by polymer aggregation. PFEBTs show fluorescence turn-on rather than fluorescence quenching upon complexation with proteins. Both electrostatic and hydrophobic interactions between PFEBTs and proteins are found to improve the polymer fluorescence, the extent of which is dependent on the nature of the polymer and the protein. Changes in solution pH adjust the net charges of proteins, providing an effective way to manipulate electrostatic interactions and in turn the increment in the polymer fluorescence. In addition, the effect of protein digestion on the fluorescence of polymer/protein complexes is probed. The results indicate that electrostatic interaction induced polymer fluorescence increase cannot be substantially reduced through cleaving protein into peptide fragments. In contrast, hydrophobic interactions, mainly determined by the hydrophobicity of proteins, can be minimized by digestion, imparting a light-off signature for the polymer/protein complexes. This study thus not only highlights the opportunities of exerting nonspecific interactions for protein sensing but also reveals significant implications for biosensor design. © 2010 American Chemical Society.
Source Title: Journal of Physical Chemistry B
URI: http://scholarbank.nus.edu.sg/handle/10635/63931
ISSN: 15206106
DOI: 10.1021/jp906433u
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