Amantadine
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | < | + | <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 12: | Line 12: | ||
===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
| |||||||||||
Pharmacokinetics
For Pharmacokinetic Data References, See: References |
||||||||||||||||||||||||||||||||||
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
