Thermodynamic aspects of hydrophobicity and biological QSAR.
A protein contains a large amount of water molecules, and the nature of the interactions of the water molecules with a protein play an important role in the thermodynamics of the ligand binding process. In this paper, thermodynamic aspects of drug-receptor interactions, enthalpy-entropy compensation or reinforcement, hydrophobicity, and biological 2D- and 3D-QSAR are discussed. Comparisons of the thermodynamic QSAR of phenyl esters of N-benzoyl L-alanine in phosphate buffer and pentanol provide useful insight for the ligand-enzyme interactions.
Kim
K H
KH
Department of Structural Biology, Abbott Laboratories, Abbott Park, IL 60061-6100, USA.
D000409:Alanine / Q000031:analogs & derivatives / Q000737:chemistry; D001665:Binding Sites; D003198:Computer Simulation; D017076:Computer-Aided Design; D015195:Drug Design; D008024:Ligands; D008958:Models, Molecular; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D021281:Quantitative Structure-Activity Relationship; D011955:Receptors, Drug / Q000737:chemistry / Q000378:metabolism; D012997:Solvents; D013816:Thermodynamics; D014867:Water
D008024:Ligands; D011506:Proteins; D011955:Receptors, Drug; D012997:Solvents; D014867:Water; C047207:N-benzoylalanine; D000409:Alanine