Devapamil

Last updated
Devapamil
Devapamil.svg
Names
IUPAC name
(RS)-2-(3,4-dimethoxyphenyl)-2-isopropyl-5-[2-(3-methoxyphenyl)ethyl-methylamino]pentanenitrile
Identifiers
3D model (JSmol)
ChEBI
ChEMBL
ChemSpider
PubChem CID
UNII
  • InChI=1/C26H36N2O3/c1-20(2)26(19-27,22-11-12-24(30-5)25(18-22)31-6)14-8-15-28(3)16-13-21-9-7-10-23(17-21)29-4/h7,9-12,17-18,20H,8,13-16H2,1-6H3
    Key: VMVKIDPOEOLUFS-UHFFFAOYAV
  • N#CC(c1cc(OC)c(OC)cc1)(CCCN(CCc2cccc(OC)c2)C)C(C)C
Properties
C26H36N2O3
Molar mass 424.57564
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).

Devapamil is a calcium channel blocker. It is also known as desmethoxyverapamil, which is a phenylalkylamine (PAA) derivative. [1] Devapamil not only inhibits by blocking the calcium gated channels, but also by depolarizing the membrane during the sodium-potassium exchanges. [2]

Contents

Structure

Devapamil consists of two aromatic rings with methoxy substituents connected by an alkylamine chain increasing flexibility and overall potency. [3]

Animal studies

Devapamil in rats can be used to decrease glutathione levels and increase oxidation of lipids, which makes it effective in preclusion of ulcers caused by stress. [4] [5] The medical characteristics of this drug, and other phenylalkylamines, depends greatly on the state of the calcium channels being targeted which results in a greater affinity and drug efficiency. [6]

Related Research Articles

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<span class="mw-page-title-main">Oxidative stress</span> Free radical toxicity

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Calcium/calmodulin-dependent protein kinase type IV is an enzyme that in humans is encoded by the CAMK4 gene.

<span class="mw-page-title-main">SYT1</span> Protein-coding gene in the species Homo sapiens

Synaptotagmin-1 is a protein that in humans is encoded by the SYT1 gene.

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Calsenilin is a protein that in humans is encoded by the KCNIP3 gene.

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<span class="mw-page-title-main">CLCA1</span> Protein-coding gene in the species Homo sapiens

Chloride channel accessory 1 is a protein that in humans is encoded by the CLCA1 gene.

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<span class="mw-page-title-main">CACNB4</span> Protein-coding gene in the species Homo sapiens

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<span class="mw-page-title-main">CLCA2</span> Protein-coding gene in the species Homo sapiens

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<span class="mw-page-title-main">ITPR3</span> Protein-coding gene in the species Homo sapiens

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The Calcium-Dependent Chloride Channel (Ca-ClC) proteins (or calcium-activated chloride channels, are heterogeneous groups of ligand-gated ion channels for chloride that have been identified in many epithelial and endothelial cell types as well as in smooth muscle cells. They include proteins from several structurally different families: chloride channel accessory, bestrophin, and calcium-dependent chloride channel anoctamin channels ANO1 is highly expressed in human gastrointestinal interstitial cells of Cajal, which are proteins which serve as intestinal pacemakers for peristalsis. In addition to their role as chloride channels some CLCA proteins function as adhesion molecules and may also have roles as tumour suppressors. These eukaryotic proteins are "required for normal electrolyte and fluid secretion, olfactory perception, and neuronal and smooth muscle excitability" in animals. Members of the Ca-CIC family are generally 600 to 1000 amino acyl residues in length and exhibit 7 to 10 transmembrane segments.

References

  1. Erdmann R, Lüttgau HC (June 1989). "The effect of the phenylalkylamine D888 (devapamil) on force and Ca2+ current in isolated frog skeletal muscle fibres". The Journal of Physiology. 413 (1): 521–41. doi:10.1113/jphysiol.1989.sp017667. PMC   1189114 . PMID   2557440.
  2. Dierkes PW, Wende V, Hochstrate P, Schlue WR (July 2004). "L-type Ca2+ channel antagonists block voltage-dependent Ca2+ channels in identified leech neurons". Brain Research. 1013 (2): 159–67. doi:10.1016/j.brainres.2004.03.038. PMID   15193524. S2CID   22004238.
  3. Cheng RC, Tikhonov DB, Zhorov BS (October 2009). "Structural model for phenylalkylamine binding to L-type calcium channels". The Journal of Biological Chemistry. 284 (41): 28332–42. doi: 10.1074/jbc.M109.027326 . PMC   2788883 . PMID   19700404.
  4. Alican I, Toker F, Arbak S, Yegen BC, Yalçin AS, Oktay S (August 1994). "Gastric lipid peroxidation, glutathione and calcium channel blockers in the stress-induced ulcer model in rats". Pharmacological Research. 30 (2): 123–35. doi:10.1016/1043-6618(94)80004-9. PMID   7816741.
  5. Hung CR (May 2004). "Protective effects of lysozyme chloride and reduced glutathione on betel quid chewing-produced gastric oxidative stress and haemorrhagic ulcer in rats". Inflammopharmacology. 12 (2): 115–29. doi:10.1163/1568560041352284. PMID   15265315. S2CID   860321.
  6. Cheng RC, Tikhonov DB, Zhorov BS (October 2009). "Structural model for phenylalkylamine binding to L-type calcium channels". The Journal of Biological Chemistry. 284 (41): 28332–42. doi: 10.1074/jbc.M109.027326 . PMC   2788883 . PMID   19700404.