Amprenavir: Difference between revisions

{{Short description|Chemical compound}}

{{Refimprove|date=December 2009}}

| verifiedrevid = 457129255

| image = Amprenavir structure.svg

| licence_EU = yes

| pregnancy_category =

| legal_status = Rx-only

| routes_of_administration = Oral ([[Capsule (pharmacy)|capsules]])

| bioavailability =

| metabolism = [[Liver|Hepatic]]

| elimination_half-life = 7.1–10.6 hours

| CAS_number_Ref = {{cascite|correct|??}}

| ATC_supplemental =

| ChEBI_Ref = {{ebicite|correct|EBI}}

| ChEMBL_Ref = {{ebicite|correct|EBI}}

| NIAID_ChemDB = 006080

| C=25 | H=35

| N=3 | O=6

| S=1

'''Amprenavir''' (original brand name '''Agenerase''', [[GlaxoSmithKline]]) is a [[protease inhibitor (pharmacology)|protease inhibitor]] used to treat [[HIV infection]]. It was approved by the [[Food and Drug Administration]] on April 15, 1999, for twice-a-day dosing instead of needing to be taken every eight hours. The convenient dosing came at a price, as the dose required is 1,200&nbsp;mg, delivered in 8 (eight) very large 150 mg gel capsules or 24 (twenty-four) 50 mg gel capsules twice daily.<ref name = "PI">{{cite web|title=Agenerase (amprenavir) Capsules. Full Prescribing Information. Section Dosage and Administration|url=http://www.accessdata.fda.gov/drugsatfda_docs/label/2002/21007s11,21039s10lbl.pdf|website=US Food and Drug Administration|publisher=GlaxoSmithKline and Vertex Pharmaceuticals Inc.|access-date=29 November 2015}}</ref>

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It was patented in 1992 and approved for medical use in 1999.<ref name=Fis2006>{{cite book | vauthors = Fischer J, Ganellin CR |title=Analogue-based Drug Discovery |date=2006 |publisher=John Wiley & Sons |isbn=9783527607495 |page=509 |url=https://books.google.com/books?id=FjKfqkaKkAAC&pg=PA509 |language=en}}</ref> Production of amprenavir was discontinued by the manufacturer on December 31, 2004; a [[prodrug]] version ([[fosamprenavir]]), is available.

==Background==

[[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}}

== External links ==

* [http://www.ebi.ac.uk/pdbe-srv/PDBeXplore/ligand/?ligand=478 Amprenavir bound to proteins] in the [[Protein Data Bank]]

[[Category:Abandoned drugs]]

[[Category:Carbamates]]

[[Category:CYP3A4 inhibitors]]

[[Category:HIV protease inhibitors]]

[[Category:1992 in science]]

[[Category:Isobutyl compounds]]

[[Category:4-Aminophenyl compounds]]