Abstract
Rotational diffusion of fluorescein family nanomarkers (initial fluorescein and its halogenated derivatives, eosin and erythrosine) in solutions of human serum albumin (HSA) was studied at various pH values. In solutions of HSA, the degree of fluorescence polarization, rotational relaxation time, and Einstein radius of nanomarkers are larger and the rotational diffusion coefficient of nanomarkers smaller than in solutions without the protein. An increase in the electronegativity of atoms in the structural formulas of nanomarkers increases the degree of polarization of their fluorescence, decreases the coefficient of their rotational diffusion, and increases rotational relaxation time and the effective Einstein radius.
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