Licochalcone A bound to bovine serum albumin: a spectroscopic , photophysical, and structural study (Articolo in rivista)

Type

• Prodotto della ricerca (Classe)
• Articolo in rivista (Classe)

Label

• Licochalcone A bound to bovine serum albumin: a spectroscopic , photophysical, and structural study (Articolo in rivista) (literal)

Anno

• 2009-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

• 10.1039/b823227j (literal)

Alternative label

• S. Monti, I. Manet, F. Manoli, S. Ottani, G. Marconi (2009)
  Licochalcone A bound to bovine serum albumin: a spectroscopic , photophysical, and structural study
  in Photochemical & photobiological sciences (Print)
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• S. Monti, I. Manet, F. Manoli, S. Ottani, G. Marconi (literal)

Pagina inizio

• 805 (literal)

Pagina fine

• 813 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 8 (literal)

Rivista

• Photochemical & photobiological sciences (Rivista)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali

• 9 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo

• 6 (literal)

Note

• ISI Web of Science (WOS) (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• S. Monti, I. Manet, F. Manoli, S. Ottani, G. Marconi: ISOF-CNR (literal)

Titolo

• Licochalcone A bound to bovine serum albumin: a spectroscopic , photophysical, and structural study (literal)

Abstract

• The interaction of Licochalcone A (LA) with bovine serum albumin (BSA) was studied by circular dichroism (CD), UV-Vis absorption, fluorescence and laser. ash photolysis. The most stable 1 : 1 and 2 : 1 LA: BSA complexes were spectroscopically characterized. Two protein sites of similar affinity are involved in the LA association with both stoichiometries. The fluorescence quantum yield was found to be higher by ca. one order of magnitude for bound LA than for the free molecule. The emission lifetime strongly depended on the protein site. Binding induced an increase in the radiative rate constant for one location and a decrease of the non-radiative rate in the other location. Two LA triplets were evidenced in the protein environment, the first one shorter-lived and the second one longer-lived than in buffer. The BSA fluorescence was quenched in the complexes. FRET was found to be inefficient. Molecular mechanics (MM), molecular dynamics (MD) and quantum mechanical calculations of rotational strength combined with CD data afforded the likely structures of the complexes. One, involving the interaction of LA with Trp212 in domain II, was able to account for most of the observed photophysical effects. MM and MD calculations also showed LA associates in domain III, the lowest energy complex being one with the drug close to Tyr409. (literal)

Prodotto di

• Institute for organic syntheses and photoreactivity (ISOF) (Istituto)
• Studio delle interazioni legando-recettore in sistemi modello mediante metodi spettroscopici e fotofisici (LEGARE) (PM.P06.005.002) (Modulo)

Autore CNR

• ILSE GERT MANET (Unità di personale interno)
• FRANCESCO MANOLI (Persona)
• SANDRA MONTI (Persona)
• STEFANO OTTANI (Unità di personale interno)
• GIANCARLO MARCONI (Unità di personale interno)

Incoming links:

Prodotto

• Institute for organic syntheses and photoreactivity (ISOF) (Istituto)
• Studio delle interazioni legando-recettore in sistemi modello mediante metodi spettroscopici e fotofisici (LEGARE) (PM.P06.005.002) (Modulo)

Autore CNR di

• STEFANO OTTANI (Unità di personale interno)
• GIANCARLO MARCONI (Unità di personale interno)
• ILSE GERT MANET (Unità di personale interno)
• FRANCESCO MANOLI (Persona)
• SANDRA MONTI (Persona)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• Photochemical & photobiological sciences (Rivista)