Biopolym. Cell. 1992; 8(4):20-30.
http://dx.doi.org/10.7124/bc.00032A
Structure and Function of Biopolymers
Dipeptides conteining m- and p-fluorophenylalanine. Synthesis separation on optical isomers and study of their substrate properties towards thrombin
1Poyarkova S. A., 1Kukhar V. P., 1Kolicheva M. T., 1Hrapunov S. N., 1Dragan A. I.
  1. Institute of Bioorganic Chemistry and Petrochemistry, NAS of Ukraine
    1, Murmans'ka Str., Kyiv, Ukraine, 02094

Abstract

In order to search of new substrates and inhibitors for thrombin DL-and LL-stereoisomers of dipeptide Tos-Phe-(X)-Arg-OCH3 (where X-tn- or p-fluorophenylalanine) were synthesized by classical methods of peptide chemistry from racemate tosylfluorophenylalanine. Tos-L-Phe(pF)-Arg-OCH3 showed substrate's activation at concentration [S] >KM and inhibition by substrate at [S] < KM Tos-L-Phe(mF)-Arg-OCH3 has no bioregulatory effect. Isomers containing D-fluorophenylalanine are not split by thrombin. Study of absorption spectrum and difference in spectrums of fluorescence showed different conformational flexibility of DL and LL isomers. Bathochromic shift in absorption spectrum and fluorescent spectrums of m-fluorophenylalanine is differ from the same of dipeptide, containing p-fluorophenylalanine. The connection between conformational flexibility and substrate's properties of dipeptides is discussed.
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