Muramyl dipeptide

Muramyl dipeptide (MDP) is a peptide derived from the bacterial cell wall component peptidoglycan. It is the smallest naturally occurring peptidoglycan molecule capable of activating the immune system and has been extensively studied for its immunomodulatory properties.

Structure

Muramyl dipeptide is composed of a muramic acid residue linked to a short dipeptide, typically L-alanine-D-isoglutamine. The muramic acid component is a unique sugar found only in bacterial cell walls, which contributes to the molecule's immunostimulatory activity.

Biological activity

MDP is recognized by the NOD2 protein, a member of the NOD-like receptor family of pattern recognition receptors. Upon binding to MDP, NOD2 undergoes a conformational change that allows it to interact with other proteins and initiate a signal transduction pathway leading to the activation of nuclear factor kappa B (NF-κB), a transcription factor that regulates the expression of numerous genes involved in immune and inflammatory responses.

Therapeutic potential

Due to its ability to stimulate the immune system, MDP has been investigated for potential use in vaccine adjuvants and cancer immunotherapy. However, its clinical use has been limited by its potent pro-inflammatory activity, which can cause severe side effects.

See also

• Immunostimulant
• Adjuvant
• Pattern recognition receptor
• NOD-like receptor
• Nuclear factor kappa B

References

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Muramyl dipeptide Resources
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