Amantadine: Difference between revisions
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< | <StructureSection load='' size='340' side='right' caption='Amantadine, also known as Symmetrel ([[2kqt]])' scene=Amantadine/Amantadine/1'> | ||
===Better Known as: Symmetrel=== | ===Better Known as: Symmetrel=== | ||
* Marketed By: Endo Pharmaceuticals | * Marketed By: Endo Pharmaceuticals | ||
| Line 7: | Line 7: | ||
* 1994 Sales: N/A | * 1994 Sales: N/A | ||
* Importance: One of the the first treatments approved by the FDA and the first approved for treatment of [[Influenza]] Infections. Nearly 100% of influenza viruses had developed resistance to rimantadine, and it is no longer recommended as a treatment for the flu. Interestingly, in 1969 it was also discovered that Amantadine helped reduce the symptoms of Parkinson's Disease. | * Importance: One of the the first treatments approved by the FDA and the first approved for treatment of [[Influenza]] Infections. Nearly 100% of influenza viruses had developed resistance to rimantadine, and it is no longer recommended as a treatment for the flu. Interestingly, in 1969 it was also discovered that Amantadine helped reduce the symptoms of Parkinson's Disease. | ||
* | * See [[Pharmaceutical Drugs]] for more information about other drugs and disorders. | ||
* (<scene name="Amantadine/Amantadine/1">Restore initial scene</scene>). | |||
===Mechanism of Action=== | ===Mechanism of Action=== | ||
The [[Influenza]] A Virus viral envelope is dotted with various [[ion channels]] including [[M2 Proton Channel|M2 Proton Channels]]. The <scene name='Amantadine/M2/1'>M2 protein</scene> plays a critical role in the life cycle of the Influenza virus. It enables hydrogen ions to enter the virion form the endosome. The result of this is a more acidic environment within the virus, causing dissociation of the viral matrix protein M1 from the ribonucleoprotein RNP. Dissociation of the viral matrix protein is a crucial step in uncoating of the virus and exposing its contents to the cytoplasm of the host cell, allowing the virus to hijack the cellular machinery to replicate. <scene name='Amantadine/Bound/1'>Amantadine binds to the pore</scene> formed by the M2 protein, utilizing Val 27, Ala 30 and Ser 31 in each M2 protein chain, effectively disabling the protein from transferring protons into the viral particle.<ref>PMID: 18235503</ref> | |||
</StructureSection> | |||
===Pharmacokinetics=== | ===Pharmacokinetics=== | ||
<table style="background: cellspacing="0px" align="" cellpadding="0px" width="42%"> | |||
<tr> | |||
<td style="width:100%; vertical-align:top;border-width:0px; border-style:inset"> | |||
<div style="height:100%; width: 100%"> | |||
{{:M2 Proton Channel Inhibitor Pharmacokinetics}} | |||
</div> | |||
</td> | |||
</tr> | |||
</table> | |||
===References=== | ===References=== | ||
Latest revision as of 12:08, 14 January 2024
Better Known as: Symmetrel
Mechanism of ActionThe Influenza A Virus viral envelope is dotted with various ion channels including M2 Proton Channels. The plays a critical role in the life cycle of the Influenza virus. It enables hydrogen ions to enter the virion form the endosome. The result of this is a more acidic environment within the virus, causing dissociation of the viral matrix protein M1 from the ribonucleoprotein RNP. Dissociation of the viral matrix protein is a crucial step in uncoating of the virus and exposing its contents to the cytoplasm of the host cell, allowing the virus to hijack the cellular machinery to replicate. formed by the M2 protein, utilizing Val 27, Ala 30 and Ser 31 in each M2 protein chain, effectively disabling the protein from transferring protons into the viral particle.[1] |
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Pharmacokinetics
For Pharmacokinetic Data References, See: References |
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References
- ↑ Schnell JR, Chou JJ. Structure and mechanism of the M2 proton channel of influenza A virus. Nature. 2008 Jan 31;451(7178):591-5. PMID:18235503 doi:10.1038/nature06531