Abstract
Objective: The main aim of the present study was to develop a sensitive liquid chromatography–electrospray ionization–tandem mass spectrometric technique for the quantitation of amprenavir in human plasma.
 Methods: Chromatographic separation was achieved on a reversed-phase Symmetry C18 (50 mm×4.6 mm, 3.5 μm) column with isocratic elution by acetonitrile and 0.1% v/v formic acid in the ratio of 90:10 v/v as mobile phase. Chromatographic peaks were resolved with 0.7 ml/min flow rate. Drug was extracted with ethyl acetate solvent by liquid–liquid extraction method. Monitoring of transition of m/z 506.2 and 71.0 for amprenavir and 628 and 421 for methyl-indinavir was made on multiple reaction monitoring.
 Results: Calibration curve of amprenavir was linear over 1–600 ng/ml concentration range with regression coefficient (r2) value of >0.99. The % relative standard deviation values were <8.5% for interday and intraday precision and accuracy. The method has excellent recovery, and the percentage recovery values of lower quality control (QC), median QC, and higher QC samples were 101.86%, 102.8%, and 99.28%, respectively.
 Conclusion: The drug was stable for more time at variable stability conditions, and method was successfully applicable to regular analysis of amprenavir in biological matrices.
Highlights
Amprenavir is a protease inhibitor with activity against human immunodeficiency virus type-1 (HIV-1)
A bioanalytical LC-MS/MS method for the amprenavir was developed and validated with methyl-indinavir as Internal standard (IS). This method has excellent recovery, accuracy, and precision compared with existed methods for the analysis of drug in human plasma samples
The drug was extracted from plasma samples by liquid–liquid extraction method with ethyl acetate as an extraction solvent
Summary
Amprenavir is a protease inhibitor with activity against human immunodeficiency virus type-1 (HIV-1). HIV-1 protease is an enzyme required for the proteolytic cleavage of the viral polyprotein precursors into the individual functional proteins found in infectious HIV-1. Amprenavir binds to the protease active site and inhibits the activity of the enzyme. This inhibition prevents cleavage of the viral polyproteins resulting in the formation of immature non-infectious viral particles. Protease inhibitors are almost always used in combination with at least two other anti-HIV drugs. Amprenavir inhibits the HIV viral proteinase enzyme which prevents cleavage of the gag-pol polyprotein, resulting in noninfectious, immature viral particles. The two major metabolites result from oxidation of the tetrahydrofuran and aniline moieties. Glucuronide conjugates of oxidized metabolites have been identified as minor metabolites in urine and feces [4,5]
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