Computational Study of KNI-272, a Potent Inhibitor of HIV-1 Protease: On the Mechanism of Preorganization
β Scribed by David, Laurent; Luo, Ray; Head, Martha S.; Gilson, Michael K.
- Book ID
- 126306482
- Publisher
- American Chemical Society
- Year
- 1999
- Tongue
- English
- Weight
- 281 KB
- Volume
- 103
- Category
- Article
- ISSN
- 0022-3654
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The effects of dose on the pharmacokinetic characteristics of KNI-272 were evaluated in rats after intravenous (iv) administration. The plasma kinetics of KNI-272 were dose-independent within a dose range of 1.0 to 10.0 mg/kg. However, when the dose was increased to 50.0 mg/kg, the area under the pl
does not contain a basic amine as do Saquinovir and JG-365, for example it should be easier to desolvate, which also assists in binding. The relationship between KNI-272, JG-365, Saquinovir, and P X proline-containing substrate also is 1
The binding characteristics of KNI-272, a potent and selective human immunodeficiency virus (HIV) protease inhibitor, were evaluated in rat and human plasma, and in solutions of human a,-acid glycoprotein (AAG) and human serum albumin (HSA). The unbound fractions (F,) of KNI-272 were 12.13 and 2.24%