title: Exploring biomolecular recognition using optical biosensors.
abstract: Understanding the basic forces that determine molecular recognition helps to elucidate mechanisms of biological processes and facilitates discovery of innovative biotechnological methods and materials for therapeutics, diagnostics, and separation science. The ability to measure interaction properties of biological macromolecules quantitatively across a wide range of affinity, size, and purity is a growing need of studies aimed at characterizing biomolecular interactions and the structural elements that drive them. Optical biosensors have provided an increasingly impactful technology for such biomolecular interaction analyses. These biosensors record the binding and dissociation of macromolecules in real time by transducing the accumulation of mass of an analyte molecule at the sensor surface coated with ligand molecule into an optical signal. Interactions of analytes and ligands can be analyzed at a microscale and without the need to label either interactant. Sensors enable the detection of bimolecular interaction as well as multimolecular assembly. Most notably, the method is quantitative and kinetic, enabling determination of both steady-state and dynamic parameters of interaction. This article describes the basic methodology of optical biosensors and presents several examples of its use to investigate such biomolecular systems as cytokine growth factor-receptor recognition, coagulation factor assembly, and virus-cell docking.
authors.affiliation: Department of Medicine, School of Medicine, University of Pennsylvania, Philadelphia 19104, USA.
authors.forename: G
authors.initials: G
authors.lastname: Canziani
authors.forename: W
authors.initials: W
authors.lastname: Zhang
authors.forename: D
authors.initials: D
authors.lastname: Cines
authors.forename: A
authors.initials: A
authors.lastname: Rux
authors.forename: S
authors.initials: S
authors.lastname: Willis
authors.forename: G
authors.initials: G
authors.lastname: Cohen
authors.forename: R
authors.initials: R
authors.lastname: Eisenberg
authors.forename: I
authors.initials: I
authors.lastname: Chaiken
mesh_terms: D016477:Artifacts; D001665:Binding Sites; D015374:Biosensing Techniques; D015942:Factor VIIa / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D015848:Interleukin-5 / Q000737:chemistry / Q000378:metabolism; D008024:Ligands; D010958:Plasminogen / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D018123:Receptors, Interleukin / Q000737:chemistry / Q000378:metabolism; D053649:Receptors, Interleukin-5; D012680:Sensitivity and Specificity; D020349:Surface Plasmon Resonance / Q000295:instrumentation / Q000379:methods*; D013925:Thromboplastin / Q000737:chemistry / Q000378:metabolism
chemical_list: D015848:Interleukin-5; D008024:Ligands; D011506:Proteins; D018123:Receptors, Interleukin; D053649:Receptors, Interleukin-5; D010958:Plasminogen; D013925:Thromboplastin; D015942:Factor VIIa