Surface-enhanced Raman scattering and fluorescence spectroscopy reveal molecular interactions of all-trans retinoic acid and RAR gamma ligand-binding domain.
Surface-enhanced Raman scattering and fluorescence were used to investigate the interactions of all-trans retinoic acid with the gamma-type retinoic acid receptor. Raman data revealed a significant attenuation in intensity of the bands originating from the retinoic acid polyenic chain upon receptor binding, with the spectrum being dominantly that of the beta-ionone ring. Fluorescence measurements supported the hydrophobic character of the ligand binding. These novel spectroscopic results are fully consistent with the published X-ray crystallographic data and suggest that these techniques may be valuable additional tools to characterize the interactions of agonists and antagonists with residues in the ligand-binding pockets of retinoid receptor homo- and heterodimers.
Morjani
H
H
Laboratoire de Spectroscopie Biomoléculaire, IFR53, UFR de Pharmacie, Université de Reims Champagne-Ardenne, France.
Beljebbar
A
A
Sockalingum
G D
GD
Mattioli
T A
TA
Bonnier
D
D
Gronemeyer
H
H
Manfait
M
M
D001665:Binding Sites; D018360:Crystallography, X-Ray; D018168:Receptors, Retinoic Acid / Q000737:chemistry* / Q000378:metabolism*; D013050:Spectrometry, Fluorescence / Q000379:methods*; D013059:Spectrum Analysis, Raman / Q000379:methods*; D014212:Tretinoin / Q000737:chemistry* / Q000378:metabolism; D000097768:Retinoic Acid Receptor gamma
D018168:Receptors, Retinoic Acid; D014212:Tretinoin; D000097768:Retinoic Acid Receptor gamma