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%
Thermodynamic dissection of the binding energetics of KNI-272, a potent HIV-1 protease inhibitor
β Scribed by Adrian Velazquez-Campoy; Irene Luque; Matthew J. Todd; Mark Milutinovich; Yoshiaki Kiso; Ernesto Freire
- Book ID
- 111753841
- Publisher
- Cold Spring Harbor Laboratory Press
- Year
- 2000
- Tongue
- English
- Weight
- 344 KB
- Volume
- 9
- Category
- Article
- ISSN
- 0961-8368
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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