60803-67-0Relevant academic research and scientific papers
Hydrophobic parameters ? of amino-acid side chains from the partitioning of N-acetyl-amino-acid amides
Fauchere, Jean-Luc,Pliska, Vladimir
, p. 369 - 376 (2007/10/02)
A hydrophobic parameter for the side chain of each of the twenty naturally occuring amino-acids was estimated quantitatively by partitioning of their N-acetyl-amino-acid amides (CH3CO-NH-CH(R)-CONH2, R=variable side chain) in octanol/water.Suitable forms of the derivatives were synthesized chemically where necessary.The new series affords reliable distribution coefficients especially for polar amino-acids.A set of Hansch side chain parameters ? obtained for the twenty common amino-acids, for half-cystine as well as for the extremly lipophilic amino-acids carboranylalanine and adamantylalanine.It is found that these hydrophobicity indices, obtained at neutral pH, are tightly correlated with the degree of solvent exposure of the side chain in globular proteins and it is proposed that they be used in future biophysical and pharmacological studies.
