Journal
DYES AND PIGMENTS
Volume 184, Issue -, Pages -Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.dyepig.2020.108873
Keywords
Squaraine; Turn-on; UV-Vis; Fluorescence; Binding; Protein
Funding
- University of Torino
- Fondazione CRT [2019 RF. 2019.2260]
- Compagnia di San Paolo (Bando ex-post Anno 2018)
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The study investigated the binding of different squaraine dyes with proteins such as transferrin, fibrinogen, trypsin, and pepsin, and explored the protein-dye interaction mechanism and quantum yield of the complexes. It was found that the surface hydrophobicity of proteins plays a significant role in the fluorescence turn-on response of squaraine dyes, especially for those with shorter alkyl chains.
Proteins are essential constituents of living organisms. The increased development of fluorescent probes with proper selectivity offers opportunities to explore the roles of proteins in physiological functions. Squaraine dyes have demonstrated to be valuable fluorescent probes given their ability to turn-on their fluorescence in response to specific proteins. Here we investigate the binding of four different squaraines with commercially available transferrin, fibrinogen, trypsin, pepsin and a generic protease. The protein-dye interaction was studied by means of UV-Vis and fluorescence spectroscopy. The association (K-A) and dissociation (K-D) constants were determined based on the turn-on response of squaraines in presence of the proteins, and the quantum yield of the complexes was measured. The protein's surface hydrophobicity seems to play an important role on the fluorescence turn-on response of the squaraines, especially for those with shorter alkyl chains.
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