:Muramyl dipeptide

{{update|date=December 2023}}

{{Chembox

| verifiedrevid = 400318991

| ImageFile=Muramyl dipeptide.png

| ImageSize=200px

| IUPACName= (4R)-4-[ [(2S)-2-[ [(2R)-2-[(2R,5S)-3-acetamido-2,5-dihydroxy-6-(hydroxymethyl)oxan-4-yl]oxypropanoyl]amino]propanoyl]amino]-5-amino-5-oxopentanoic acid|OtherNames=Acetylmuramyl-Alanyl-Isoglutamine

|Section1={{Chembox Identifiers

| IUPHAR_ligand = 5024

| ChemSpiderID_Ref = {{chemspidercite|correct|chemspider}}

| ChemSpiderID = 9794910

| InChI = 1/C19H32N4O11/c1-7(17(30)23-10(16(20)29)4-5-12(26)27)21-18(31)8(2)33-15-13(22-9(3)25)19(32)34-11(6-24)14(15)28/h7-8,10-11,13-15,19,24,28,32H,4-6H2,1-3H3,(H2,20,29)(H,21,31)(H,22,25)(H,23,30)(H,26,27)/t7-,8+,10+,11+,13+,14+,15+,19?/m0/s1

| InChIKey = BSOQXXWZTUDTEL-QAQREVAFBN

| StdInChI_Ref = {{stdinchicite|correct|chemspider}}

| StdInChI = 1S/C19H32N4O11/c1-7(17(30)23-10(16(20)29)4-5-12(26)27)21-18(31)8(2)33-15-13(22-9(3)25)19(32)34-11(6-24)14(15)28/h7-8,10-11,13-15,19,24,28,32H,4-6H2,1-3H3,(H2,20,29)(H,21,31)(H,22,25)(H,23,30)(H,26,27)/t7-,8+,10+,11+,13+,14+,15+,19?/m0/s1

| StdInChIKey_Ref = {{stdinchicite|correct|chemspider}}

| StdInChIKey = BSOQXXWZTUDTEL-QAQREVAFSA-N

| CASNo_Ref = {{cascite|correct|CAS}}

| CASNo=53678-77-6

| UNII_Ref = {{fdacite|correct|FDA}}

| UNII = 2U7S2HVO96

| PubChem = 11620162

| SMILES = O=C(N)[C@H](NC(=O)[C@@H](NC(=O)[C@H](O[C@H]1[C@H](O)[C@H](OC(O)[C@@H]1NC(=O)C)CO)C)C)CCC(=O)O

| MeSHName=Muramyl+dipeptide

}}

|Section2={{Chembox Properties

| Formula=C₁₉H₃₂N₄O₁₁

| MolarMass=492.47758

| Appearance=

| Density=

| MeltingPt=

| BoilingPt=

| Solubility=

}}

|Section3={{Chembox Hazards

| MainHazards=

| FlashPt=

| AutoignitionPt =

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Muramyl dipeptide is a component of bacterial peptidoglycan, a recognition structure or activator for nucleotide-binding oligomerization domain 2 (NOD2) protein.{{cite journal | vauthors = Inohara N, Ogura Y, Fontalba A, Gutierrez O, Pons F, Crespo J, Fukase K, Inamura S, Kusumoto S, Hashimoto M, Foster SJ, Moran AP, Fernandez-Luna JL, Nuñez G | display-authors = 6 | title = Host recognition of bacterial muramyl dipeptide mediated through NOD2. Implications for Crohn's disease | journal = The Journal of Biological Chemistry | volume = 278 | issue = 8 | pages = 5509–5512 | date = February 2003 | pmid = 12514169 | doi = 10.1074/jbc.C200673200 | doi-access = free | hdl = 10379/9336 | hdl-access = free }} 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. 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.{{cite journal | vauthors = Martinon F, Agostini L, Meylan E, Tschopp J | title = Identification of bacterial muramyl dipeptide as activator of the NALP3/cryopyrin inflammasome | journal = Current Biology | volume = 14 | issue = 21 | pages = 1929–1934 | date = November 2004 | pmid = 15530394 | doi = 10.1016/j.cub.2004.10.027 | s2cid = 13728991 | doi-access = free }}

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,{{cite journal | vauthors = Inohara N, Ogura Y, Fontalba A, Gutierrez O, Pons F, Crespo J, Fukase K, Inamura S, Kusumoto S, Hashimoto M, Foster SJ, Moran AP, Fernandez-Luna JL, Nuñez G | display-authors = 6 | title = Host recognition of bacterial muramyl dipeptide mediated through NOD2. Implications for Crohn's disease | journal = The Journal of Biological Chemistry | volume = 278 | issue = 8 | pages = 5509–5512 | date = February 2003 | pmid = 12514169 | doi = 10.1074/jbc.c200673200 | doi-access = free | hdl = 10379/9336 | hdl-access = free }} 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.{{cite journal | vauthors = Li X, Yu J, Xu S, Wang N, Yang H, Yan Z, Cheng G, Liu G | display-authors = 6 | title = Chemical conjugation of muramyl dipeptide and paclitaxel to explore the combination of immunotherapy and chemotherapy for cancer | journal = Glycoconjugate Journal | volume = 25 | issue = 5 | pages = 415–425 | date = July 2008 | pmid = 18161023 | doi = 10.1007/s10719-007-9095-3 | s2cid = 19058605 }} Experiments published in 2008 showed that muramyl dipeptide is involved in a molecular pathway in mice that conferred protection from colitis.{{cite journal | vauthors = Watanabe T, Asano N, Murray PJ, Ozato K, Tailor P, Fuss IJ, Kitani A, Strober W | display-authors = 6 | title = Muramyl dipeptide activation of nucleotide-binding oligomerization domain 2 protects mice from experimental colitis | journal = The Journal of Clinical Investigation | volume = 118 | issue = 2 | pages = 545–559 | date = February 2008 | pmid = 18188453 | pmc = 2176188 | doi = 10.1172/JCI33145 }}