RELACORILANT

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Search structure


Synonyms	CORT125134 Cort 125134 Cort-125134 Relacorilant
Status
Molecule Category	UNKNOWN
UNII	2158753C7E


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

Structure


InChI Key	WANIDIGFXJFFEL-SANMLTNESA-N
Smiles	Cn1cc(S(=O)(=O)N2CCC3=Cc4c(cnn4-c4ccc(F)cc4)C[C@]3(C(=O)c3cc(C(F)(F)F)ccn3)C2)cn1
InChI	InChI=1S/C27H22F4N6O3S/c1-35-15-22(14-33-35)41(39,40)36-9-7-18-11-24-17(13-34-37(24)21-4-2-20(28)3-5-21)12-26(18,16-36)25(38)23-10-19(6-8-32-23)27(29,30)31/h2-6,8,10-11,13-15H,7,9,12,16H2,1H3/t26-/m0/s1

Physicochemical Descriptors

Property Name	Value
Molecular Formula	C27H22F4N6O3S
Molecular Weight	586.57
AlogP	4.06
Hydrogen Bond Acceptor	8.0
Hydrogen Bond Donor	0.0
Number of Rotational Bond	5.0
Polar Surface Area	102.98
Molecular species	NEUTRAL
Aromatic Rings	4.0
Heavy Atoms	41.0

Bioactivity

Mechanism of Action	Action	Reference
Glucocorticoid receptor antagonist	ANTAGONIST	Other


Protein: Glucocorticoid receptor Description: Glucocorticoid receptor Organism : Homo sapiens P04150 ENSG00000113580

Targets	EC50(nM)	IC50(nM)	Kd(nM)	Ki(nM)	Inhibition(%)
Enzyme Cytochrome P450 Cytochrome P450 family 2 Cytochrome P450 family 2C Cytochrome P450 2C19	-	8000	-	-	-
Enzyme Cytochrome P450 Cytochrome P450 family 2 Cytochrome P450 family 2C Cytochrome P450 2C8	-	210	-	-	-
Enzyme Cytochrome P450 Cytochrome P450 family 2 Cytochrome P450 family 2C Cytochrome P450 2C9	-	2000	-	-	-
Enzyme Cytochrome P450 Cytochrome P450 family 2 Cytochrome P450 family 2D Cytochrome P450 2D6	-	9000	-	-	-
Enzyme Cytochrome P450 Cytochrome P450 family 3 Cytochrome P450 family 3A Cytochrome P450 3A4	-	1300	-	-	-
Enzyme Cytochrome P450 Cytochrome P450 family 3 Cytochrome P450 family 3A Cytochrome P450 3A5	-	4900	-	-	-
Transcription factor Nuclear receptor Nuclear hormone receptor subfamily 3 Nuclear hormone receptor subfamily 3 group C Nuclear hormone receptor subfamily 3 group C member 1	-	-	-	7-81	100

Assay Description	Organism	Bioactivity	Reference
Antagonist activity at glucocorticoid receptor in human HepG2 cells assessed as inhibition of dexamethasone-induced tyrosine amino transferase activity preincubated for 30 mins followed by dexamethasone addition measured after 20 hrs	Homo sapiens	7.2 nM
Inhibition of radioligand binding to progesterone receptor (unknown origin) at 1 uM relative to control	Homo sapiens	10.0 %
Inhibition of radioligand binding to androgen receptor (unknown origin) at 1 uM relative to control	Homo sapiens	10.0 %
Inhibition of radioligand binding to estrogen receptor (unknown origin) at 1 uM relative to control	Homo sapiens	10.0 %
Displacement of fluormone GS Red from human glucocorticoid receptor at 1 uM after 4 hrs by fluorescence polarization assay relative to control	Homo sapiens	100.0 %
Antagonist activity at monkey glucocorticoid receptor in primary hepatocytes assessed as dexamethasone-induced tyrosine amino transferase activity preincubated for 30 mins followed by dexamethasone addition measured after 20 hrs	Macaca mulatta	210.0 nM
Antagonist activity at rat glucocorticoid receptor in primary hepatocytes assessed as dexamethasone-induced tyrosine amino transferase activity preincubated for 30 mins followed by dexamethasone addition measured after 20 hrs	Rattus norvegicus	12.0 nM
Inhibition of CYP2C8 (unknown origin)	Homo sapiens	210.0 nM
Antagonist activity at glucocorticoid receptor in human primary hepatocytes assessed as inhibition of dexamethasone-induced tyrosine amino transferase activity preincubated for 30 mins followed by dexamethasone addition measured after 20 hrs	Homo sapiens	81.2 nM

Related Entries

Cross References

Resources	Reference
ChEMBL	CHEMBL4068611
DrugBank	DB14976
FDA SRS	2158753C7E
PubChem	73051463
SureChEMBL	SCHEMBL15454999
ZINC	ZINC000141949519

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).