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

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 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.

authors

Nose T,Shimohigashi Y,Ohno M,Costa T,Shimizu N,Ogino Y

doi

10.1006/bbrc.1993.1680

subject

Has Abstract

pub_date

1993-06-15 00:00:00

pages

694-9

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(83)71680-3

journal_volume

193

pub_type

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