Study of interaction of proton transfer probe 1-hydroxy-2-naphthaldehyde with serum albumins: a spectroscopic study.
J Photochem Photobiol B
; 91(1): 1-8, 2008 Apr 25.
Article
em En
| MEDLINE
| ID: mdl-18296059
ABSTRACT
In the present work, we have studied the interaction of proton transfer probe 1-hydroxy-2-naphthaldehyde (HN12) with Human Serum Albumin (HSA) and Bovine Serum Albumin (BSA) by steady state absorption and emission spectroscopy combined with time resolved fluorescence measurements. The measured binding constant (K) and free energy change (DeltaG) indicate a stronger affinity of HN12 molecule for HSA than BSA. Steady state anisotropy, excitation anisotropy and fluorescence resonance energy transfer (FRET) studies indicate that the probe molecule resides at the hydrophobic site of the protein environment.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Albumina Sérica
/
Soroalbumina Bovina
/
Naftalenos
Limite:
Animals
/
Humans
Idioma:
En
Ano de publicação:
2008
Tipo de documento:
Article