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Raman spectroscopy in comparative investigations of mechanisms of binding of three molecular probes – fluorescein, eosin, and erythrosin – to human serum albumin

✍ Scribed by I.M. Vlasova; A.M. Saletsky


Publisher
John Wiley and Sons
Year
2008
Tongue
English
Weight
116 KB
Volume
5
Category
Article
ISSN
1612-2011

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✦ Synopsis


The comparative analysis of binding of three molecular fluorescent probes (fluorescein, eosin, and erythrosin), belonging to one homologous family, to human serum albumin (HSA) is made by Raman spectroscopy method. The binding of all three probes to binding Center I of HSA is registered. The character of binding of initial probe of the given homologous family -fluorescein -to protein differs from character of binding of its halogen-derivatives (eosin and erythrosin) to protein.

The differences in binding of these three probes to HSA are determined by value of electronegativity of atoms of lateral radicals in structural formulas of probes and, therefore, by value of pK of their ionized groups.

Raman intensity, 10-5 a.u.


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