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Chemistry of Natural Compounds

, Volume 15, Issue 4, pp 484–490 | Cite as

A study of the properties of synthetic analogs of the tryptophan-containing fragment 113–121 of the basic protein of myelin

  • A. A. Gershkovich
  • V. K. Kibirev
  • S. B. Serebryanyi
  • Ya. T. Terletskaya
  • E. P. Kozulina
  • Ya. V. Belik
Article
  • 21 Downloads

Abstract

New analogs of fragment 113–121 of the basic protein of myelin were synthesized: Phe-Ser-Trp-Gly-Ala-Glu-Gly-Gln-Arg, in which the phenylalanine in the first position has been replaced by L-alanine (V) and by D-phenylalanine (IX), and also a shortened analog with the deletion of the serine in the second position (XIII) and a lengthened analog with the insertion of glycine between the phenylalanine and tryptophan (XVII). In experiments on guinea pigs, one of the compounds obtained exhibited encephalitogenic activity. The circular dichroism spectra of compounds (I) and (IX), and also of some model compounds, have been studied in order to analyze the contribution of the aromatic amino acid residues to the dichroic absorption.

Keywords

Ethyl Ester Hydrazide Tryptophan Residue DMFA Aromatic Amino Acid Residue 

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Copyright information

© Plenum Publishing Corporation 1980

Authors and Affiliations

  • A. A. Gershkovich
  • V. K. Kibirev
  • S. B. Serebryanyi
  • Ya. T. Terletskaya
  • E. P. Kozulina
  • Ya. V. Belik

There are no affiliations available

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