IMP-1088
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| CAS_number = 2059148-82-0
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| PubChem = 132274735
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| ChemSpiderID = 65326081
| UNII = ZT62NQ6YEV
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| ChEMBL = 4445137
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| PDB_ligand = KFK
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| C=25 | H=29 | F=2 | N=5 | O=1
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| SMILES = CC1=C(C(=NN1C)C)CCOC2=C(C=CC(=C2F)F)C3=CC4=C(C=C3)N(N=C4CN(C)C)C
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| StdInChI = InChI=1S/C25H29F2N5O/c1-15-18(16(2)31(5)28-15)11-12-33-25-19(8-9-21(26)24(25)27)17-7-10-23-20(13-17)22(14-30(3)4)29-32(23)6/h7-10,13H,11-12,14H2,1-6H3
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IMP-1088 is an enzyme inhibitor of the human N-myristoyltransferases NMT1 and NMT2. It prevents the production of infectious virus particles by targeting host cell machinery rather than the virus itself. Specifically, it inhibits the host's NMT enzymes, blocking the myristoylation of viral proteins required for capsid assembly. Since this strategy acts on host proteins, it is thought to carry a lower risk of viral resistance.{{cite web | vauthors = Borman S | title = Agent stops common cold virus replication | url = https://cen.acs.org/pharmaceuticals/drug-discovery/Agent-stops-common-cold-virus/96/i21?hootPostID=8a78f5ab938bf07977e9703b0a487e37 | website = Chemical & Engineering News | access-date = 20 May 2018 }}{{cite news | vauthors = Houser K | title = A team of researchers may have actually found a cure to the common cold | date = 19 May 2018 | url = http://www.businessinsider.com/researchers-may-have-actually-found-a-cure-to-the-common-cold-2018-5 | access-date = 20 May 2018 | work = Business Insider }}
Antiviral activity
IMP-1088 blocks the replication of viruses that rely on myristoylated proteins for their life cycle, including poxviruses, mammarenaviruses, and rhinoviruses.{{cite journal | vauthors = Mousnier A, Bell AS, Swieboda DP, Morales-Sanfrutos J, Pérez-Dorado I, Brannigan JA, Newman J, Ritzefeld M, Hutton JA, Guedán A, Asfor AS, Robinson SW, Hopkins-Navratilova I, Wilkinson AJ, Johnston SL, Leatherbarrow RJ, Tuthill TJ, Solari R, Tate EW | title = Fragment-derived inhibitors of human N-myristoyltransferase block capsid assembly and replication of the common cold virus | journal = Nature Chemistry | volume = 10 | issue = 6 | pages = 599–606 | date = June 2018 | pmid = 29760414 | pmc = 6015761 | doi = 10.1038/s41557-018-0039-2 | bibcode = 2018NatCh..10..599M }}{{cite journal | vauthors = Witwit H, Betancourt CA, Cubitt B, Khafaji R, Kowalski H, Jackson N, Ye C, Martinez-Sobrido L, de la Torre JC | title = Cellular N-Myristoyl Transferases Are Required for Mammarenavirus Multiplication | journal = Viruses | volume = 16 | issue = 9 | pages = 1362 | date = August 2024 | pmid = 39339839 | pmc = 11436053 | doi = 10.3390/v16091362 | doi-access = free }}{{Cite journal | vauthors = Witwit H, Cubitt B, Khafaji R, Castro EM, Goicoechea M, Lorenzo MM, Blasco R, Martinez-Sobrido L, de la Torre JC | title = Repurposing Drugs for Synergistic Combination Therapies to Counteract Monkeypox Virus Tecovirimat Resistance | journal = Viruses | volume = 17 | issue = 1 | pages = 92 | date = January 2025 | pmid = 39861882 | pmc = 11769280 | doi = 10.3390/v17010092 | language = en | doi-access = free | issn = 1999-4915 }} This approach has been explored for potential treatment of monkeypox, Lassa fever, and the common cold.
= Poxviruses =
Research applications
In addition to its antiviral potential, IMP-1088 has been used as a research tool to study viral protein function. It has been shown that myristoylation and oligomerization are not required for the Z matrix protein’s dose-dependent inhibitory effect on viral ribonucleoprotein (vRNP) activity.{{Cite journal | vauthors = Witwit H, de la Torre JC | title = Mammarenavirus Z Protein Myristoylation and Oligomerization Are Not Required for Its Dose-Dependent Inhibitory Effect on vRNP Activity | journal = BioChem | volume = 5 | issue = 2 | pages = 10 | date = 2025-04-29 | doi = 10.3390/biochem5020010 | language = en | doi-access = free | issn = 2673-6411 }}