FOSTAMATINIB

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Search structure


Synonyms	Fostamatinib R-788 R-788 FREE ACID R-935788 R-935788 FREE ACID R788 FREE ACID R935788 FREE ACID
Status
Molecule Category	Free-form
ATC	B02BX09
UNII	SQ8A3S5101


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

Structure


InChI Key	GKDRMWXFWHEQQT-UHFFFAOYSA-N
Smiles	COc1cc(Nc2ncc(F)c(Nc3ccc4c(n3)N(COP(=O)(O)O)C(=O)C(C)(C)O4)n2)cc(OC)c1OC
InChI	InChI=1S/C23H26FN6O9P/c1-23(2)21(31)30(11-38-40(32,33)34)20-14(39-23)6-7-17(28-20)27-19-13(24)10-25-22(29-19)26-12-8-15(35-3)18(37-5)16(9-12)36-4/h6-10H,11H2,1-5H3,(H2,32,33,34)(H2,25,26,27,28,29)

Physicochemical Descriptors

Property Name	Value
Molecular Formula	C23H26FN6O9P
Molecular Weight	580.47
AlogP	3.09
Hydrogen Bond Acceptor	12.0
Hydrogen Bond Donor	4.0
Number of Rotational Bond	10.0
Polar Surface Area	186.72
Molecular species	ACID
Aromatic Rings	3.0
Heavy Atoms	40.0

Bioactivity

Mechanism of Action	Action	Reference
Tyrosine-protein kinase SYK inhibitor	INHIBITOR	PubMed


Protein: Tyrosine-protein kinase SYK Description: Tyrosine-protein kinase SYK Organism : Homo sapiens P43405 ENSG00000165025

Targets	EC50(nM)	IC50(nM)	Kd(nM)	Ki(nM)	Inhibition(%)
Enzyme Kinase Protein Kinase TK protein kinase group Tyrosine protein kinase Syk family	-	17-12000	-	-	-

Assay Description	Organism	Bioactivity	Reference
Inhibition of SYK in human Ramos cells	Homo sapiens	267.0 nM
Inhibition of human recombinant truncated SYK (360 to 365 amino acid residues) using N-terminally biotinylated EPEGDYEEVLE peptide as substrate assessed as inhibition of [33P]-ATP incorporation incubated for 10 mins prior to substrate addition measured after 15 mins by scintillation counting	Homo sapiens	17.0 nM
Antiarthritic activity in bovine type-2 collagen-induced DBA1/J mouse arthritic model assessed as inhibition of arthritis scores at 30 mg/kg, po bid administered for 14 days starting day after second immunization relative to control	Mus musculus	58.0 %
Kinobeads (epsilon), multiple immobilized ATP-competitive broad spectrum kinase inhibitors, used to assess residual binding of ~300 proteins simultaneously from cell lysate in the presence of a compound. Quantitative readout performed by mass spectrometry.	Homo sapiens	300.0 nM
Kinobeads (epsilon), multiple immobilized ATP-competitive broad spectrum kinase inhibitors, used to assess residual binding of ~300 proteins simultaneously from cell lysate in the presence of a compound. Quantitative readout performed by mass spectrometry.	Homo sapiens	843.0 nM
Kinobeads (epsilon), multiple immobilized ATP-competitive broad spectrum kinase inhibitors, used to assess residual binding of ~300 proteins simultaneously from cell lysate in the presence of a compound. Quantitative readout performed by mass spectrometry.	Homo sapiens	41.0 nM
Kinobeads (epsilon), multiple immobilized ATP-competitive broad spectrum kinase inhibitors, used to assess residual binding of ~300 proteins simultaneously from cell lysate in the presence of a compound. Quantitative readout performed by mass spectrometry.	Homo sapiens	570.0 nM
Kinobeads (epsilon), multiple immobilized ATP-competitive broad spectrum kinase inhibitors, used to assess residual binding of ~300 proteins simultaneously from cell lysate in the presence of a compound. Quantitative readout performed by mass spectrometry.	Homo sapiens	160.0 nM

Related Entries

Cross References

Resources	Reference
ChEMBL	CHEMBL2103830
DrugBank	DB12010
DrugCentral	5280
FDA SRS	SQ8A3S5101
Guide to Pharmacology	7796
PDB	2RC
PubChem	11671467
SureChEMBL	SCHEMBL1201371
ZINC	ZINC000043131420

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).