Affinity
Ligand Synthesis
Deuterated Tocopherols
Fluorescent Analogues
Tocopherol
Binding to Proteins and Enzymes
The first view you should see is a "stick"-structure of alpha-tocopherol, coloured CPK, such that the oxygen atoms are red, the carbons light grey and the hydrogens white. ( Click here to go back to the CPK model after using the buttons shown below)
a-Tocopherol consists of a chroman ring and a phytyl sidechain. Here the chroman is coloured red | The phytyl tail is coloured green. | a-Tocopherol contains three aryl methyl groups at C-5, C-7, and C-8, here coloured purple. (The oxygens of the chroman are coloured red) |
There are two sites of stereochemistry on the phytyl sidechain at C-4' and C-8'. Both are of R-absolute stereochemistry in natural a-tocopherol | The stereochemistry at C-2 is also of the R-configuration and is particularly important for affinity to the a-tocopherol transfer proteins (a-TTPs) | A spacefilling model of a-tocopherol with the important methyl groups in purple and the chroman oxygens in red |
They have an excellent site providing general information on tocopherol structrues and bioactiviy