The mechanism of binding of molecular probe fluorescein to molecules of human serum albumin was studied by the Raman spectroscopy method. The position of binding Center on human serum albumin molecule for fluorescein is determined. The amino acid residues of albumin molecule, participating in bindin
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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The mechanism of binding of molecular probe eosin to molecules of human serum albumin was studied by the Raman spectroscopy method. The position of binding center on human serum albumin molecule for eosin is determined. The amino acid residues of albumin molecule, participating in binding of eosin a