Tipranavir: Difference between revisions
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< | <StructureSection load='' size='340' side='right' caption='Tipranavir, better known as Aptivus, ([[2o4p]])' scene='Tipranavir/Tipranavir/1'> | ||
===Better Known as: Aptivus=== | ===Better Known as: Aptivus=== | ||
* Marketed By: Boehringer-Ingelheim<br /> | * Marketed By: Boehringer-Ingelheim<br /> | ||
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* 2009 Sales: N/A | * 2009 Sales: N/A | ||
* Importance: It was the ninth [[HIV Protease]] inhibitor approved by the FDA for treatment of HIV. It is a very potent inhibitor, and is often recommended for patients who have become resistant to other treatments, but also has a relatively harsh side-effect profile. | * Importance: It was the ninth [[HIV Protease]] inhibitor approved by the FDA for treatment of HIV. It is a very potent inhibitor, and is often recommended for patients who have become resistant to other treatments, but also has a relatively harsh side-effect profile. | ||
* | * See [[Pharmaceutical Drugs]] for more information about other drugs and diseases. | ||
===Mechanism of Action=== | ===Mechanism of Action=== | ||
When [[HIV]] infects a host, it directs the synthesis of several polyproteins. The maturation of the virus to its infectious form requires that these polyproteins be cleaved to their component proteins by [[HIV Protease]]. The subunits of <scene name='Tipranavir/Prot/1'>HIV Protease</scene> come together to form a catalytic tunnel capable of binding the nascent peptides and cleaving them into their mature form. Within this tunnel lies <scene name='Tipranavir/Cat/3'>two Asp-Thr-Gly conserved sequences</scene>, which contain the <scene name='Tipranavir/Catas/1'>catalytic Asp residues</scene>. These catalytic Asp residues carry out the hydrolytic cleavage of the polyprotein. | When [[HIV]] infects a host, it directs the synthesis of several polyproteins. The maturation of the virus to its infectious form requires that these polyproteins be cleaved to their component proteins by [[HIV Protease]]. The subunits of <scene name='Tipranavir/Prot/1'>HIV Protease</scene> come together to form a catalytic tunnel capable of binding the nascent peptides and cleaving them into their mature form. Within this tunnel lies <scene name='Tipranavir/Cat/3'>two Asp-Thr-Gly conserved sequences</scene>, which contain the <scene name='Tipranavir/Catas/1'>catalytic Asp residues</scene>. These catalytic Asp residues carry out the hydrolytic cleavage of the polyprotein. Tipranavir <scene name='Tipranavir/Bound/1'>binds with great specificity</scene> to these conserved sequences within the HIV Protease tunnel, preventing the nascent polyproteins from entering. Unable to actively cleave the nascent proteins into their infectious form, HIV is unable to mature and proliferate, allowing the patients immune system to fight off the infection more easily.<ref>PMID:1799632</ref><ref>doi:10.1038/nrd1907</ref> | ||
===Drug Resistance=== | ===Drug Resistance=== | ||
The biggest difficulty with treating [[HIV]] is the rapidity at which it mutates and becomes resistant to treatments. To view a comprehensive and interactive analysis of the mutations which confer drug resistance to [[HIV Protease]], See: [[HIV Protease Inhibitor Resistance Profile]] | The biggest difficulty with treating [[HIV]] is the rapidity at which it mutates and becomes resistant to treatments. To view a comprehensive and interactive analysis of the mutations which confer drug resistance to [[HIV Protease]], See: [[HIV Protease Inhibitor Resistance Profile]] | ||
</StructureSection> | |||
===Pharmacokinetics=== | ===Pharmacokinetics=== | ||
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{{:HIV Protease Inhibitor Pharmacokinetics}} | |||
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===References=== | ===References=== | ||