Paper
1 March 2010 Near-infrared fluorophores as biomolecular probes
Gabor Patonay, Garfield Beckford, Lucjan Strekowski, Maged Henary, Yonathan Merid
Author Affiliations +
Abstract
Near-Infrared (NIR) fluorescence has been valuable in analytical and bioanalytical chemistry. NIR probes and labels have been used for several applications, including hydrophobicity of protein binding sites, DNA sequencing, immunoassays, CE separations, etc. The NIR region (700-1100 nm) has advantages for the spectroscopist due to the inherently lower background interference from the biological matrix and the high molar absorptivities of NIR chromophores. During the studies we report here several NIR dyes were prepared to determine the role of the hydrophobicity of NIR dyes and their charge in binding to amino acids and proteins, e.g., serum albumins. We synthesized NIR dye homologs containing the same chromophore but substituents of varying hydrophobicity. Hydrophobic moieties were represented by alkyl and aryl groups. These NIR dyes of varying hydrophobicity exhibited varying degrees of H-aggregation in aqueous solution indicating that the degree of H-aggregation could be used as an indicator to predict binding characteristics to serum albumins. In order to understand what factors may be important in the binding process, spectral behavior of these varying hydrophobicity dyes were examined in the presence of amino acids. Typical dye structures that exhibit large binding constants to biomolecules were compared in order to optimize applications utilizing non-covalent interactions.
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Gabor Patonay, Garfield Beckford, Lucjan Strekowski, Maged Henary, and Yonathan Merid "Near-infrared fluorophores as biomolecular probes", Proc. SPIE 7576, Reporters, Markers, Dyes, Nanoparticles, and Molecular Probes for Biomedical Applications II, 757607 (1 March 2010); https://doi.org/10.1117/12.849451
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KEYWORDS
Near infrared

Luminescence

Molecules

Proteins

Chemistry

Chromophores

Dysprosium

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