Muramyl_dipeptide
Muramyl dipeptide
Chemical compound
Muramyl dipeptide is a component of bacterial peptidoglycan, a recognition structure or activator for nucleotide-binding oligomerization domain 2 (NOD2) protein.[1] It is a constituent of both Gram-positive and Gram-negative bacteria composed of N-acetylmuramic acid linked by its lactic acid moiety to the N-terminus of an L-alanine D-isoglutamine dipeptide.[1] It can be recognized by the immune system as a pathogen-associated molecular pattern and activate the NALP3 inflammasome which, in turn, leads to cytokine activation, IL-1α and IL-1β especially.[2]
This article needs to be updated. (December 2023) |
Human NOD2 protein of the nucleotide-binding leucine-rich repeat family, is a cytoplasmic receptor involved in host innate immune system defense. Mutations in the CARD15 gene encoding NOD2 protein have been observed in Crohn's disease patients,[3] decreasing the immune systems of these patients ability to recognize muramyl dipeptide. Analogues of muramyl dipeptide and their potential for immune response therapies in cancer and disease are being investigated.[4] Experiments published in 2008 showed that muramyl dipeptide is involved in a molecular pathway in mice that conferred protection from colitis.[5]