ID: ALA1644701

Max Phase: Preclinical

Molecular Formula: HNNa2O8S2

Molecular Weight: 209.16

Molecule Type: Small molecule

Representations

Synonyms (1): Sodium Iminodisulfate
Synonyms from Alternative Forms(1):

Canonical SMILES:  O=S(=O)([O-])ONOS(=O)(=O)[O-].[Na+].[Na+]

Standard InChI:  InChI=1S/H3NO8S2.2Na/c2-10(3,4)8-1-9-11(5,6)7;;/h1H,(H,2,3,4)(H,5,6,7);;/q;2*+1/p-2

Standard InChI Key:  BOPVDICBCJWYHX-UHFFFAOYSA-L

Molecule Features

Natural Product: No

Oral: No

Chemical Probe: No

Parenteral: No

Molecule Type: Small molecule

Topical: No

First In Class: No

Black Box: No

Chirality: No

Availability: No

Prodrug: No

Properties

Molecular Weight: 209.16

Molecular Weight (Monoisotopic): 208.9300

AlogP: -1.96

#Rotatable Bonds: 4

Polar Surface Area: 139.23

Molecular Species: ACID

HBA: 7

HBD: 3

#RO5 Violations: 0

HBA (Lipinski): 9

HBD (Lipinski): 3

#RO5 Violations (Lipinski): 0

CX Acidic pKa: -4.02

CX Basic pKa: 0.81

CX LogP: -4.74

CX LogD: -5.89

Aromatic Rings: 0

Heavy Atoms: 11

QED Weighted: 0.36

Np Likeness Score: 0.22

References

1. Burghout P, Vullo D, Scozzafava A, Hermans PW, Supuran CT..  (2011)  Inhibition of the β-carbonic anhydrase from Streptococcus pneumoniae by inorganic anions and small molecules: Toward innovative drug design of antiinfectives?,  19  (1): [PMID:21163660] [10.1016/j.bmc.2010.11.031]

2. Vullo D, De Luca V, Scozzafava A, Carginale V, Rossi M, Supuran CT, Capasso C..  (2012)  Anion inhibition studies of the fastest carbonic anhydrase (CA) known, the extremo-CA from the bacterium Sulfurihydrogenibium azorense.,  22  (23): [PMID:23072866] [10.1016/j.bmcl.2012.09.065]

3. Monti SM, De Simone G, Dathan NA, Ludwig M, Vullo D, Scozzafava A, Capasso C, Supuran CT..  (2013)  Kinetic and anion inhibition studies of a β-carbonic anhydrase (FbiCA 1) from the C4 plant Flaveria bidentis.,  23  (6): [PMID:23414801] [10.1016/j.bmcl.2013.01.087]

4. Del Prete S, Vullo D, De Luca V, Carginale V, Scozzafava A, Supuran CT, Capasso C..  (2013)  A highly catalytically active γ-carbonic anhydrase from the pathogenic anaerobe Porphyromonas gingivalis and its inhibition profile with anions and small molecules.,  23  (14): [PMID:23769640] [10.1016/j.bmcl.2013.05.063]

5. Pan P, Vermelho AB, Scozzafava A, Parkkila S, Capasso C, Supuran CT..  (2013)  Anion inhibition studies of the α-carbonic anhydrase from the protozoan pathogen Trypanosoma cruzi, the causative agent of Chagas disease.,  21  (15): [PMID:23790722] [10.1016/j.bmc.2013.05.058]

6. Vullo D, Sai Kumar RS, Scozzafava A, Capasso C, Ferry JG, Supuran CT..  (2013)  Anion inhibition studies of a β-carbonic anhydrase from Clostridium perfringens.,  23  (24): [PMID:24210500] [10.1016/j.bmcl.2013.10.037]

7. De Luca V, Vullo D, Del Prete S, Carginale V, Scozzafava A, Osman SM, AlOthman Z, Supuran CT, Capasso C..  (2015)  Cloning, characterization and anion inhibition studies of a new γ-carbonic anhydrase from the Antarctic bacterium Pseudoalteromonas haloplanktis.,  23  (15): [PMID:26145820] [10.1016/j.bmc.2015.06.021]

8. Pinard MA, Lotlikar SR, Boone CD, Vullo D, Supuran CT, Patrauchan MA, McKenna R..  (2015)  Structure and inhibition studies of a type II beta-carbonic anhydrase psCA3 from Pseudomonas aeruginosa.,  23  (15): [PMID:26068018] [10.1016/j.bmc.2015.05.029]

Source

Source(1):

• Scientific Literature