New analogue of cyclolinopeptide B modified by amphiphilic residue of alpha-hydroxymethylmethionine.
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.
Witkowska
Renata
R
Institute of Organic Chemistry, Technical University of Łódz, Łódz, Poland.
Donigiewicz
Anna
A
Zimecki
Michał
M
Zabrocki
Janusz
J
D000818:Animals; D000917:Antibody Formation; D004912:Erythrocytes / Q000276:immunology; D005260:Female; D006968:Hypersensitivity, Delayed; D007111:Immunity, Cellular; D008297:Male; D008715:Methionine / Q000031:analogs & derivatives* / Q000737:chemistry; D051379:Mice; D008808:Mice, Inbred CBA; D008958:Models, Molecular; D010047:Ovalbumin / Q000276:immunology; D010456:Peptides, Cyclic / Q000138:chemical synthesis / Q000737:chemistry* / Q000494:pharmacology; D012756:Sheep / Q000276:immunology; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D010456:Peptides, Cyclic; C019421:hydroxymethylmethionine; D010047:Ovalbumin; D008715:Methionine