MARIBAVIR

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Search structure


Synonyms	1263-W-94 1263W94 Maribavir
Status
Molecule Category	UNKNOWN
ATC	J05AX10
UNII	PTB4X93HE1
EPA CompTox	DTXSID60170091


Active Pharmaceutical Ingredients Bioactive chemicals	Exact Similarity SubStructure	Threshold (%) >= 70

Structure


InChI Key	KJFBVJALEQWJBS-XUXIUFHCSA-N
Smiles	CC(C)Nc1nc2cc(Cl)c(Cl)cc2n1[C@H]1O[C@@H](CO)[C@H](O)[C@@H]1O
InChI	InChI=1S/C15H19Cl2N3O4/c1-6(2)18-15-19-9-3-7(16)8(17)4-10(9)20(15)14-13(23)12(22)11(5-21)24-14/h3-4,6,11-14,21-23H,5H2,1-2H3,(H,18,19)/t11-,12-,13-,14-/m0/s1

Physicochemical Descriptors

Property Name	Value
Molecular Formula	C15H19Cl2N3O4
Molecular Weight	376.24
AlogP	1.77
Hydrogen Bond Acceptor	7.0
Hydrogen Bond Donor	4.0
Number of Rotational Bond	4.0
Polar Surface Area	99.77
Molecular species	NEUTRAL
Aromatic Rings	2.0
Heavy Atoms	24.0

Bioactivity

Mechanism of Action	Action	Reference
Phosphotransferase pUL97 inhibitor	INHIBITOR	PubMed PubMed PubMed PubMed

Assay Description	Organism	Bioactivity	Reference
Antiviral activity against Human cytomegalovirus T2211 expressing wild type UL27 kinase by SEAP yield reduction assay	Human herpesvirus 5	95.0 nM
Antiviral activity against Human cytomegalovirus T2899 expressing wild type UL27 kinase with N289D, D298G, N300G, P307L,V310A, D351N, I367V mutant gene by SEAP yield reduction assay	Human herpesvirus 5	84.0 nM
Antiviral activity against Human cytomegalovirus T2981 expressing UL27 kinase with W153R mutant gene by SEAP yield reduction assay	Human herpesvirus 5	160.0 nM
Antiviral activity against Human cytomegalovirus T2767 expressing UL27 kinase with L193Fmutant gene by SEAP yield reduction assay	Human herpesvirus 5	240.0 nM
Antiviral activity against Human cytomegalovirus T2867 expressing UL27 kinase with A269T mutant gene by SEAP yield reduction assay	Human herpesvirus 5	190.0 nM
Antiviral activity against Human cytomegalovirus T3053 expressing UL27 kinase with V353E mutant gene by SEAP yield reduction assay	Human herpesvirus 5	200.0 nM
Antiviral activity against Human cytomegalovirus T3037 expressing UL27 kinase with L426F mutant gene by SEAP yield reduction assay	Human herpesvirus 5	210.0 nM
Antiviral activity against Human cytomegalovirus T3020 expressing UL27 kinase with E22stop gene by SEAP yield reduction assay	Human herpesvirus 5	190.0 nM
Antiviral activity against Human cytomegalovirus T2898 expressing UL27 kinase with W362stop gene N289D, D298G, N300G, P307L, V310A, D351N, I367V mutant gene by SEAP yield reduction assay	Human herpesvirus 5	210.0 nM
Antiviral activity against Human cytomegalovirus T3019 expressing UL27 kinase with 218delC mutant gene by SEAP yield reduction assay	Human herpesvirus 5	230.0 nM
Antiviral activity against Human cytomegalovirus T2931 expressing UL27 kinase 301 to 311 deletion with frame shift mutation at 311 codon by SEAP yield reduction assay	Human herpesvirus 5	290.0 nM
Antiviral activity determined as inhibition of SARS-CoV-2 induced cytotoxicity of Caco-2 cells at 10 uM after 48 hours by high content imaging	Homo sapiens	27.61 %
SARS-CoV-2 3CL-Pro protease inhibition percentage at 20µM by FRET kind of response from peptide substrate	Severe acute respiratory syndrome coronavirus 2	10.57 %
Antiviral activity determined as inhibition of SARS-CoV-2 induced cytotoxicity of VERO-6 cells at 10 uM after 48 hours exposure to 0.01 MOI SARS CoV-2 virus by high content imaging	Chlorocebus sabaeus	0.11 %		Antiviral activity determined as inhibition of SARS-CoV-2 induced cytotoxicity of VERO-6 cells at 10 uM after 48 hours exposure to 0.01 MOI SARS CoV-2 virus by high content imaging	Chlorocebus sabaeus	0.11 %

Cross References

Resources	Reference
ChEMBL	CHEMBL515408
DrugBank	DB06234
FDA SRS	PTB4X93HE1
PubChem	471161
SureChEMBL	SCHEMBL791309
ZINC	ZINC000003824412

CONTENTS

PREMIER has received funding from the Innovative Medicines Initiative 2 Joint Undertaking (JU) under grant agreement No 875508. The JU receives support from the EU’s Horizon 2020 research and innovation programme and the European Federation of Pharmaceutical Industries and Associations (EFPIA). The views reflect only the authors’ perspective and the JU is not responsible for any use that may be made of the information this manuscript contains.

Elements of the website have been developed under projects PREMIER and the Biocenter Finland Drug Discovery and Chemical Biology network. CSC-IT is thanked for providing computational resources. Content of the website is provided without guarantee for correctness. Data has been collected and integrated from multiple public sources, for the largest: FDA, HUGO Gene Nomenclature Committee, ChEMBL, IUPHAR/BPS guide to pharmacology, Reactome, UniProt, and Ensembl. Credit is given to Ensembl for collecting species images (provided under public domain licences such as Wikimedia and NHGRI).