Hydrophobicity--shake flasks, protein folding and drug discovery.
Hydrophobic interactions are some of the most important interactions in nature. They are the primary driving force in a number of phenomena. This is mostly an entropic effect and can account for a number of biophysical events such as protein-protein or protein-ligand binding that are of immense importance in drug design. The earliest studies on this phenomenon can be dated back to the end of the 19(th) century when Meyer and Overton independently correlated the hydrophobic nature of gases to their anesthetic potency. Since then, significant progress has been made in this realm of science. This review briefly traces the history of hydrophobicity research along with the theoretical estimation of partition coefficients. Finally, the application of hydrophobicity estimation methods in the field of drug design and protein folding is discussed.
Sarkar
Aurijit
A
Department of Medicinal Chemistry, Box 980540, Virginia Commonwealth University, Richmond VA, 23298-0540, USA.
Kellogg
Glen E
GE
D015195:Drug Design; D055808:Drug Discovery; D057927:Hydrophobic and Hydrophilic Interactions; D004364:Pharmaceutical Preparations / Q000737:chemistry*; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D021281:Quantitative Structure-Activity Relationship
D004364:Pharmaceutical Preparations; D011506:Proteins