HIV-1 protease inhibitors: Enthalpic versus entropic optimization of the binding affinity

Medicine & Life Sciences

• Human immunodeficiency virus 1 p16 protease 100%
• HIV Protease Inhibitors 97%
• Entropy 80%
• Thermodynamics 27%
• Hydrophobic and Hydrophilic Interactions 24%
• Drug Resistance 20%
• Lead 20%
• Binding Sites 17%
• Temperature 15%
• Ligands 15%
• Mutation 12%
• Pharmaceutical Preparations 9%
• glutamyl-aspartyl-leucine 3%

Chemical Compounds

• Protease Inhibitor 78%
• Kd 50%
• Entropy 27%
• Enthalpy 26%
• Glu-Asp-Leu 22%
• Tripeptide 12%
• Hydrophobicity 9%
• Solvation 9%
• Mutation 9%
• Binding Site 7%
• Thermodynamics 6%
• Drug 5%
• Ligand 4%