z-logo
open-access-imgOpen Access
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.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom