New analogue of cyclolinopeptide B modified by amphiphilic residue of alpha-hydroxymethylmethionine.
Author(s) -
R Witkowska,
Anna Donigiewicz,
Michał Zimecki,
Janusz Zabrocki
Publication year - 2004
Publication title -
acta biochimica polonica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.452
H-Index - 78
eISSN - 1734-154X
pISSN - 0001-527X
DOI - 10.18388/abp.2004_3597
Subject(s) - residue (chemistry) , methionine , peptide , amphiphile , chemistry , biological activity , stereochemistry , immune system , biochemistry , in vitro , amino acid , biology , organic chemistry , immunology , copolymer , polymer
In order to evaluate the role and influence of the methionine residue on the biological activity of cyclolinopeptide B, an analogue with methionine residue in position 7 replaced by the amphiphilic (S)-alpha-hydroxymethylmethionine residue was synthesized. This peptide exhibits high immunosuppressive activity in the cellular, and to a lesser degree in the humoral immune response, comparable to that of CsA. In addition, the peptide was devoid of toxicity, even at high doses.
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