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- W2074574413 abstract "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 drasticaliy (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." @default.
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- W2074574413 date "1993-06-01" @default.
- W2074574413 modified "2023-09-25" @default.
- W2074574413 title "Enhancement of Thrombin Receptor Activation by Thrombin Receptor-Derived Heptapeptide with para-Fluorophenylalanine in Place of Phenylalanine" @default.
- W2074574413 doi "https://doi.org/10.1006/bbrc.1993.1680" @default.
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