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Thermodynamic dissection of the binding energetics of KNI-272, a potent HIV-1 protease inhibitor

✍ 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 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%

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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