Synthesis and physicochemical and encephalitogenic properties of analogs of a tryptophan-containing fragment of myelin protein
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1. Analogs of the encephalitogenic nonapeptide with the substitution of glycine in the first and in the first and second positions and also with the deletion of the glutamic acid residue and the insertion of a glycine residue between the fifth and sixth positions have been synthesized.
2. An investigation of the encephalitogenic activity of the compounds synthesized has shown the necessity for a hydrophobic N-terminal amino acid, since the replacement of phenylalanine by glycine leads to the inactivation of the compound. A change in the length of the encephalitogenic determinant also leads to the loss of EAE activity.
3. The CD spectra of the peptides synthesized are identical in water, a 1% solution of SDS, and an 8 M solution of urea and do not change on heating to 50°C. It is obvious that under the conditions mentioned these compounds do not possess an ordered structure of the α-helical type of a β structure, and their dichroic absorption is due to the contribution of the aromatic side chains.
KeywordsSodium Dodecyl Sulfate Hydrazide Myelin Protein Amic Acid Aromatic Side Chain
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