Structure-function investigation of glucosaminylmuramyl peptides. Influence of chemical modification of the N-acetylglucosaminyl-N-acetylmuramyl dipeptide (GMDP) on its immunemodulatory properties in vivo and in vitro
E. A. Mescheryakova, S. V. Guryanova, E. A. Makarov, T. M. Andronova, V. T. Ivanov
M. M. Shemyakin Institute of Bioorganic Chemistry, Academy of Sciences of the USSR, Moscow
Abstract: The structure-function relationships in a series of synthetic glucosaminylmuramyl peptides – glycopeptide adjuvants of the bacterial origin – have been investigated. Modification of the N-acetylglucosaminyl-(β1–4)-N-acetylmuramyl-L-alanyl-D-isoglutamine (GMDP) molecule affects its adjuvant and pyrogenic activity in vivo. GMDP is shown to readily stimulate the synthesis of the IgG2a and IgG3 of the immunoglobulin subclasses upon the secondary immune response to the protein antigen. The adjuvant effect correlates with the comitogenic test of the reaction of splenocytes blast-transformation in the presence of B-cell mitogen. No direct dependence has been revealed between the level of the glycopeptides adjuvant action and their effect on the IL-1 production by macrophages.
Russian Journal of Bioorganic Chemistry 1991, 17 (9):1157-1165