IPRONIAZID


Synonyms	Iproniazid Iproniazide Marsilid
Status
Molecule Category	UNKNOWN
UNII	D892HFI3XA
EPA CompTox	DTXSID5023168


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

Structure


InChI Key	NYMGNSNKLVNMIA-UHFFFAOYSA-N
Smiles	CC(C)NNC(=O)c1ccncc1
InChI	InChI=1S/C9H13N3O/c1-7(2)11-12-9(13)8-3-5-10-6-4-8/h3-7,11H,1-2H3,(H,12,13)

Physicochemical Descriptors

Property Name	Value
Molecular Formula	C9H13N3O
Molecular Weight	179.22
AlogP	0.72
Hydrogen Bond Acceptor	3.0
Hydrogen Bond Donor	2.0
Number of Rotational Bond	3.0
Polar Surface Area	54.02
Molecular species	NEUTRAL
Aromatic Rings	1.0
Heavy Atoms	13.0

Bioactivity

Mechanism of Action	Action	Reference
Monoamine oxidase inhibitor	INHIBITOR	PubMed PubMed PubMed PubMed

Query Gene : ENSG00000189221

Protein : Monoamine oxidase

Description: Amine oxidase [flavin-containing] A

Organism : Homo sapiens

Query Gene : ENSG00000189221

Protein : Monoamine oxidase

Description: Amine oxidase [flavin-containing] A

Organism : Homo sapiens

Query Gene : ENSG00000189221

Protein : Monoamine oxidase

Description: Amine oxidase [flavin-containing] A

Organism : Homo sapiens

Query Gene : ENSG00000189221

Protein : Monoamine oxidase

Description: Amine oxidase [flavin-containing] A

Organism : Homo sapiens

Query Gene : ENSG00000189221

Protein : Monoamine oxidase

Description: Amine oxidase [flavin-containing] A

Organism : Homo sapiens

Query Gene : ENSG00000189221

Protein : Monoamine oxidase

Description: Amine oxidase [flavin-containing] A

Organism : Homo sapiens

Query Gene : ENSG00000189221

Protein : Monoamine oxidase

Description: Amine oxidase [flavin-containing] A

Organism : Homo sapiens

Query Gene : ENSG00000189221

Protein : Monoamine oxidase

Description: Amine oxidase [flavin-containing] A

Organism : Homo sapiens

Query Gene : ENSG00000189221

Protein : Monoamine oxidase

Description: Amine oxidase [flavin-containing] A

Organism : Homo sapiens

Query Gene : ENSG00000189221

Protein : Monoamine oxidase

Description: Amine oxidase [flavin-containing] A

Organism : Homo sapiens

Query Gene : ENSG00000189221

Protein : Monoamine oxidase

Description: Amine oxidase [flavin-containing] A

Organism : Homo sapiens

Query Gene : ENSG00000189221

Target Name : Monoamine oxidase

Organism : Homo sapiens

Query Gene : ENSG00000069535

Protein : Monoamine oxidase

Description: Amine oxidase [flavin-containing] B

Organism : Homo sapiens

Query Gene : ENSG00000069535

Protein : Monoamine oxidase

Description: Amine oxidase [flavin-containing] B

Organism : Homo sapiens

Query Gene : ENSG00000069535

Protein : Monoamine oxidase

Description: Amine oxidase [flavin-containing] B

Organism : Homo sapiens

Query Gene : ENSG00000069535

Protein : Monoamine oxidase

Description: Amine oxidase [flavin-containing] B

Organism : Homo sapiens

Query Gene : ENSG00000069535

Protein : Monoamine oxidase

Description: Amine oxidase [flavin-containing] B

Organism : Homo sapiens

Query Gene : ENSG00000069535

Protein : Monoamine oxidase

Description: Amine oxidase [flavin-containing] B

Organism : Homo sapiens

Query Gene : ENSG00000069535

Protein : Monoamine oxidase

Description: Amine oxidase [flavin-containing] B

Organism : Homo sapiens

Query Gene : ENSG00000069535

Target Name : Monoamine oxidase

Organism : Homo sapiens


Protein: Monoamine oxidase Description: Amine oxidase [flavin-containing] A Organism : Homo sapiens P21397 ENSG00000189221











Protein: Monoamine oxidase Description: Amine oxidase [flavin-containing] B Organism : Homo sapiens P27338 ENSG00000069535

Targets	EC50(nM)	IC50(nM)	Kd(nM)	Ki(nM)	Inhibition(%)
Enzyme Oxidoreductase	-	8-8960	-	-	-

Reference

Journal : Bioorg. Med. Chem. Lett.

Title : Synthesis and evaluation of 6-methyl-3-phenylcoumarins as potent and selective MAO-B inhibitors.

PubMed ID : 19628387

DOI : 10.1016/j.bmcl.2009.07.039

Year : 2009

Volume : 19

Issue : 17

First Page : 5053

Last Page : 5055

Authors : Matos MJ, Viña D, Picciau C, Orallo F, Santana L, Uriarte E.

Abstract : A series of 6-methyl-3-phenylcoumarins 3-6 were synthesized and evaluated as monoamine oxidase A and B (MAO-A and MAO-B) inhibitors. A comparative study between the three possible mono methoxy 3-phenyl derivatives and the p-hydroxy analogue is reported. The synthesis of these new resveratrol-coumarin hybrids was carried out by a Perkin reaction between the 5-methylsalicylaldehyde and the corresponding phenylacetic acids. The p-methoxy substituted compound 3 was hydrolyzed to 6 by a traditional reaction with hydriodic acid. The prepared compounds show high selectivity to the MAO-B isoenzyme, some of them with IC(50) values in the low nanomolar range. Compound 4, with the methoxy group in meta position, is the most active of this series, with an IC(50) against MAO-B of 0.80 nM, and is several times more potent and MAO-B selective than the R-(-)-deprenyl (reference compound).

Reference

Journal : Bioorg Med Chem

Title : Multifunctional thioxanthone derivatives with acetylcholinesterase, monoamine oxidases and β-amyloid aggregation inhibitory activities as potential agents against Alzheimer's disease.

PubMed ID : 28237559

DOI : 10.1016/j.bmc.2017.02.027

Year : 2017

Volume : 25

Issue : 6

First Page : 1997

Last Page : 2009

Authors : Luo L, Li Y, Qiang X, Cao Z, Xu R, Yang X, Xiao G, Song Q, Tan Z, Deng Y.

Abstract : A series of 1-hydroxyl-3-aminoalkoxy-thioxanthone derivatives were designed, synthesized and evaluated as potential multifunctional agents against Alzheimer's disease (AD). The results indicated that most of these compounds exhibited good AChE and MAOs inhibitory activities, significant inhibition of self- and Cu2+-induced Aβ1-42 aggregation, and moderate to good antioxidant activities. Specifically, compound 9e displayed high inhibitory potency toward AChE (IC50=0.59±0.02μM), MAO-A and MAO-B (IC50=1.01±0.02μM and 0.90±0.01μM respectively), excellent efficiency to block both self- and Cu2+-induced Aβ1-42 aggregation (74.8±1.2% and 87.7±1.9% at 25μM, respectively), good metal-chelating property and a low toxicity in SH-SY5Y cells. Furthermore, kinetic and molecular modeling studies revealed that compound 9e binds simultaneously to the catalytic active site and peripheral anionic site of AChE, and could penetrate the BBB. Collectively, these results suggested that 9e might be a potential multifunctional agent for further development in the treatment of AD.

Reference

Journal : Bioorg Med Chem

Title : Multifunctional thioxanthone derivatives with acetylcholinesterase, monoamine oxidases and β-amyloid aggregation inhibitory activities as potential agents against Alzheimer's disease.

PubMed ID : 28237559

DOI : 10.1016/j.bmc.2017.02.027

Year : 2017

Volume : 25

Issue : 6

First Page : 1997

Last Page : 2009

Authors : Luo L, Li Y, Qiang X, Cao Z, Xu R, Yang X, Xiao G, Song Q, Tan Z, Deng Y.

Assay Description	Organism	Bioactivity
Inhibition of human recombinant MAOB expressed in BTI cells	Homo sapiens	7.54 nM
Inhibition of recombinant human MAO-A expressed in baculovirus infected BTI insect cells using kynuramine as substrate after 30 mins by fluorimetric method	Homo sapiens	837.0 nM
Inhibition of recombinant human MAO-B expressed in baculovirus infected BTI insect cells using kynuramine as substrate after 30 mins by fluorimetric method	Homo sapiens	985.0 nM

Cross References

Resources	Reference
ChEBI	5958
ChEMBL	CHEMBL92401
DrugBank	DB04818
DrugCentral	1480
FDA SRS	D892HFI3XA
KEGG	C11777
PubChem	3748
SureChEMBL	SCHEMBL4153
ZINC	ZINC000000001579

CONTENTS

Structure
Chemical and Physical Properties
Pharmacology