Immunologically active mimetics of muramyl dipeptide

TL;DRAbstract

N-acetylmuramyl-L-alanyl-D-isoglutamine (muramyl dipeptide, MDP) is the minimal immunologically active component of the bacterial cell wall peptidoglycan [1]. In last 20 years many research groups have been concerned with the synthesis and immunological studies of derivatives of this highly active glycopeptide in order to obtain molecules with improved and more defined pharmacological profiles. Although structure-activity relationships in MDP and its analogs have been well established, rational design of immunomodulators on the basis of MDP as a lead compound is impeded by the fact that the three-dimensional structure of the receptor binding site has not yet been determined. Therefore, systematic chemical modification of the molecule and development of more constrained analogs with reduced degrees of conformational freedom provide a good opportunity to define the bioactive conformation of MDP and analogs.

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