Muramyl dipeptide (MDP) is the minimal bioactive peptidoglycan motif common to all bacteria, the essential structure required for adjuvant activity in vaccines. MDP has been shown to be recognized by NOD2, but not TLR2, nor TLR2/1 or TLR2/6 associations [1,2].
In an attempt to enhance the protective activity against bacterial infection, numerous derivatives of MDP have been synthesized. Among them, L18-MDP, a 6-O-acyl derivative with a stearoyl fatty acid, showed the highest activity [3].
In HEK-Blue™ NOD2 cells, L18-MDP was 10 times more efficient than MDP to induce NF-κB activation.
References:
- Girardin SE. et al., 2003. Nod2 is a general sensor of peptidoglycan through muramyl dipeptide (MDP) detection. J Biol Chem. 278(11):8869-72.
- Inohara N. et al., 2003. Host recognition of bacterial muramyl dipeptide mediated through NOD2. Implications for Crohn's disease.J Biol Chem. 278(8):5509-12.
- Matsumoto K. et al., 1981. Stimulation of nonspecific resistance to infection induced by 6-O-acyl muramyl dipeptide analogs in mice. Infect Immun. 32(2):748-58.
