Content deleted Content added
added Category:4-Aminophenyl compounds using HotCat |
|||
| (17 intermediate revisions by 11 users not shown) | |||
Line 1:
{{Short description|Chemical compound}}
{{Refimprove|date=December 2009}}
Line 13 ⟶ 14:
| 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]]
Line 29 ⟶ 30:
| ATC_prefix = J05
| ATC_suffix = AE05
| ATC_supplemental =
| PubChem = 65016
| DrugBank_Ref = {{drugbankcite|correct|drugbank}}
Line 49 ⟶ 50:
| N=3 | O=6
| S=1
| smiles = O=C(O[C@H]1CCOC1)N[C@@H](Cc2ccccc2)[C@H](O)CN(CC(C)C)S(=O)(=O)c3ccc(N)cc3
| StdInChI_Ref = {{stdinchicite|correct|chemspider}}
Line 57:
}}
'''Amprenavir''' (original brand name '''Agenerase''', [[GlaxoSmithKline]]) is a [[protease inhibitor (pharmacology)|protease inhibitor]] used to treat [[HIV
<!-- Society and culture -->
It was patented in 1992 and approved for medical use in 1999.<ref name=Fis2006>{{cite book |
==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.▼
▲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}}
{{clear|left}}
== References ==▼
▲==References==
{{reflist}}
== External links ==
* [http://www.ebi.ac.uk/pdbe-srv/PDBeXplore/ligand/?ligand=478 Amprenavir bound to proteins] in the [[Protein Data Bank
{{HIVpharm}}
Line 92 ⟶ 77:
[[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}}
| |||