Amantadine
From Proteopedia
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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 | ||
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* 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. | * 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> | 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%"> | <table style="background: cellspacing="0px" align="" cellpadding="0px" width="42%"> | ||
Current revision
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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
