83802-77-1Relevant articles and documents
Synthesis of the 3-o-retinoyl-l-ascorbic acid and related compounds: Characterization and reducing activity against DPPH
Yamano, Yumiko,Ito, Masayoshi
, p. 289 - 299 (2007/10/03)
Novel hybrid vitamin, 3-O-retinoyl-L-ascorbic acid (3a) was conveniently prepared by reaction of sodium L-ascorbate with retinoyl fluoride. The 3-O-acylated structure was confirmed by the comparison of spectral data of its methylated compound with those of 3-O-methyl-2-O-retinoyl-L-ascorbic acid (20) prepared from 5,6-O-isopropylidene-3-O-methyl-L-ascorbic acid. 3-O-Retinoyl-L-ascorbic acid (3a) showed a reducing activity against the stable radical, α,α-diphenyl-β-picrylhydrazyl (DPPH).
All E-10,20-methanoretinoylopsin, light-stable rhodopsin. Synthesis and spectroscopy of all E-10,20-methano- and all-E-retinoyl fluoride and their reaction with bovine opsin
Steen, R. van der,Groesbeek, M.,Amsterdam, L. J. P. van,Lugtenburg, J.,Oostrum, J. van,Grip, W. J. de
, p. 20 - 27 (2007/10/02)
In order to obtain a light-stable rhodopsin as a potential candidate for crystallization and structural X-ray analysis, we synthesized and characterized the novel all E-10,20-methanoretinoyl fluoride (2).This retinal analogue has a locked 11-cis configuration, preventing the light-induced 11-cis -> trans isomerization and binds to opsin by a stable peptide bond rather than a Schiff base. 2 reacted with (methylated) bovine opsin, forming a light- and thermo-stable pigment with λmax at 390 nm.Its opsin shift (2500 cm-1) is in the same order of magnitude as that in rhodopsin (2650 cm-1), suggesting that the mechanism for the red shift is not located in the direct vicinity of the chromophore-protein linkage.We also report the first synthesis and characterization of all-E-retinoyl fluoride (10), which failed to give a pigment on reaction with bovine opsin.
Inactivation of Bovine Opsin by all-trans-Retinoyl Fluoride
Wong, Corinne G.,Rando, Robert R.
, p. 7374 - 7375 (2007/10/02)
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