Raman spectroscopy in investigations of secondary structure of human serum albumin at binding of nanomarkers of fluorescein family |
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Authors: | I M Vlasova and A M Saletsky |
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Institution: | 1.Physical Department,Moscow State University,Moscow,Russia |
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Abstract: | The influence of binding of nanomarkers of fluorescein family to HSA on secondary structure of this protein at different values
of pH was investigated by Raman spectroscopy method. The greatest changes in secondary structure of HSA, consisting in decreasing
of α-helix sites, at binding of fluorescein to HSA occur at pH 5–6. The greatest changes in secondary structure of HSA, consisting
in decreasing of α-helix sites, at binding of eosin or erythrosin to HSA take place at values of pH, smaller 5. The differences
in changes in secondary structure of HSA at binding of these three nanomarkers are explained by dependences of binding of
nanomarkers to HSA on pH which determined by value of electronegativity of atoms of lateral radicals in structural formulas
of nanomarkers and, therefore, by value of pK of their ionized groups. |
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