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added Category:4-Aminophenyl compounds using HotCat |
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{{Short description|Chemical compound}}
{{Refimprove|date=December 2009}}
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| licence_US = Amprenavir
| pregnancy_US = C
| pregnancy_category =
| legal_status =
| routes_of_administration = Oral ([[Capsule (pharmacy)|capsules]])
<!--Pharmacokinetic data-->
| bioavailability =
| protein_bound = 90%
| metabolism = [[Liver|Hepatic]]
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| ATC_prefix = J05
| ATC_suffix = AE05
| ATC_supplemental =
| PubChem = 65016
| DrugBank_Ref = {{drugbankcite|correct|drugbank}}
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<!-- Society and culture -->
It was patented in 1992 and approved for medical use in 1999.<ref name=Fis2006>{{cite book |
==Background==
Research aimed at development of [[renin inhibitors]] as potential [[antihypertensive agents]] had led to the discovery of compounds that blocked the action of this peptide cleaving enzyme. The amino acid sequence cleaved by [[renin]] was found to be fortuitously the same as that required to produce the HIV peptide coat. Structure–activity studies on renin inhibitors proved to be of great value for developing [[HIV protease inhibitors]]. Incorporation of an [[amino alcohol]] moiety proved crucial to inhibitory activity for many of these agents. This unit is closely related to the one found in the [[statine]], an unusual amino acid that forms part of the [[pepstatin]], a fermentation product that inhibits protease enzymes.▼
[[File:3nu3 478.png|thumb|left|[[HIV-1 protease]] dimer with amprenavir (sticks) bound in the active site. PDB entry {{PDBe|3nu3}}<ref>{{cite journal | vauthors = Shen CH, Wang YF, Kovalevsky AY, Harrison RW, Weber IT | title = Amprenavir complexes with HIV-1 protease and its drug-resistant mutants altering hydrophobic clusters | journal = The FEBS Journal | volume = 277 | issue = 18 | pages = 3699–714 | date = September 2010 | pmid = 20695887 | pmc = 2975871 | doi = 10.1111/j.1742-4658.2010.07771.x }}</ref>]]
▲Research aimed at development of [[renin inhibitors]] as potential [[antihypertensive agents]] had led to the discovery of compounds that blocked the action of this peptide cleaving enzyme. The amino acid sequence cleaved by [[renin]] was found to be fortuitously the same as that required to produce the HIV peptide coat. Structure–activity studies on renin inhibitors proved to be of great value for developing [[HIV protease inhibitors]]. Incorporation of an [[amino alcohol]] moiety proved crucial to inhibitory activity for many of these agents. This unit is closely related to the one found in the [[statine]], an unusual amino acid that forms part of the [[pepstatin]], a fermentation product that inhibits protease enzymes.{{cn|date=November 2022}}
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== References ==
{{reflist}}
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[[Category:Abandoned drugs]]
[[Category:Carbamates]]
[[Category:CYP3A4 inhibitors]]
[[Category:HIV protease inhibitors]]
[[Category:Sulfonamides]]
[[Category:Tetrahydrofurans]]
[[Category:1992 in science]]
[[Category:Isobutyl compounds]]
[[Category:4-Aminophenyl compounds]]
{{Antimicrobial-stub}}
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