Molecular interaction analysis in ligand design using mass transport, kinetic and thermodynamic methods.
Ligand design in biotechnology is underpinned by the control of molecular affinity. Hence, measuring binding interactions is a key component in designing ligands for such uses as therapeutics, diagnostics, biomaterials and separation science. Mass transport, kinetic and thermodynamic methods have been used for macromolecular interaction analysis but also have potential applicability as direct methods for measuring small molecular interactions. They can enhance the ligand design process by providing the ability to choose ligands based on both their kinetic and thermodynamic binding properties.
Doyle
M L
ML
Department of Macromolecular Sciences, SmithKline Beecham, King of Prussia, PA 19406, USA.
Myszka
D G
DG
Chaiken
I M
IM
D015374:Biosensing Techniques; D002151:Calorimetry / Q000379:methods; D002846:Chromatography, Affinity / Q000379:methods; D015195:Drug Design; D007700:Kinetics; D008024:Ligands; D008958:Models, Molecular; D011506:Proteins / Q000737:chemistry / Q000378:metabolism; D013816:Thermodynamics; D017186:Titrimetry
D008024:Ligands; D011506:Proteins