http://www.cnr.it/ontology/cnr/individuo/prodotto/ID51206
Spectroscopic and molecular modeling studies on the binding of the flavonoid luteolin and human serum albumin (Articolo in rivista)
- Type
- Label
- Spectroscopic and molecular modeling studies on the binding of the flavonoid luteolin and human serum albumin (Articolo in rivista) (literal)
- Anno
- 2009-01-01T00:00:00+01:00 (literal)
- Alternative label
Z. Jurasekova(1), G Marconi(2), S. Sanchez-Cortes(2), A. Torreggiani(1) (2009)
Spectroscopic and molecular modeling studies on the binding of the flavonoid luteolin and human serum albumin
in Biopolymers (Print)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Z. Jurasekova(1), G Marconi(2), S. Sanchez-Cortes(2), A. Torreggiani(1) (literal)
- Pagina inizio
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- Rivista
- Note
- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- 1 Instituto de Estructura de la Materia, CSIC, Serrano 121, Madrid 280 06, Spain
2 Istituto I.S.O.F. (C.N.R.), via P. Gobetti 101, Bologna 401 29, Italy (literal)
- Titolo
- Spectroscopic and molecular modeling studies on the binding of the flavonoid luteolin and human serum albumin (literal)
- Abstract
- Luteolin (LUT) is a polyphenolic compound, found in a
variety of fruits, vegetables, and seeds, which has a
variety of pharmacological properties. In the present
contribution, binding of LUT to human serum albumin
(HSA), the most abundant carrier protein in the blood,
was investigated with the aim of describing the binding
mode and parameters of the interaction. The application
of circular dichroism, UV-Vis absorption, fluorescence,
Raman and surface-enhanced Raman scattering
spectroscopy combined with molecular modeling afforded
a clear picture of the association mode of LUT to
HSA.Specific interactions with protein amino acids were
evidenced. LUT was found to be associated in subdomain
IIA where an interaction with Trp-214 is established.
Hydrophobic and electrostatic interactions are the major
acting forces in the binding of LUT to HSA. The HSA
conformations were slightly altered by the drug
complexation with reduction of a-helix and increase of
b-turns structures, suggesting a partial protein unfolding.
Also the configuration of at least two disulfide bridges
were altered. Furthermore, the study of molecular
modeling afforded the binding geometry. (literal)
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