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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Enhancement of thrombin receptor activation by thrombin receptor-derived heptapeptide with para-fluorophenylalanine in place of phenylalanine.

Thrombin receptor-derived peptide SFLLRNP (one-letter amino acid code) which corresponds to the N-terminal heptapeptide of tethered ligand is able to activate thrombin receptor and to stimulate the phosphoinositide (PI) turnover. The replacement of Phe-2 by Ala eliminated this activity completely, showing the crucial role of the Phe-phenyl group in receptor activation. It was found that substitution of para-fluorophenylalanine ((p-F)Phe) for Phe-2 enhanced several times the PI-turnover activity of SFLLRNP. This is the first example to date of a substitution with one order of magnitude greater increase in receptor activation. The Phe-2/Tyr substitution diminished the activity drastically (almost 2% of SFLLRNP), indicating the importance of hydrophobicity of Phe2-phenyl. The Phe-2/Leu substitution, however, diminished also the activity (less than 2% of SFLLRNP). These results suggested that highly specific hydrophobic interaction exists between Phe-2 of the tethered ligand and its binding site in thrombin receptor.[1]

References

  1. Enhancement of thrombin receptor activation by thrombin receptor-derived heptapeptide with para-fluorophenylalanine in place of phenylalanine. Nose, T., Shimohigashi, Y., Ohno, M., Costa, T., Shimizu, N., Ogino, Y. Biochem. Biophys. Res. Commun. (1993) [Pubmed]
 
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