title: MIRG Survey 2011: snapshot of rapidly evolving label-free technologies used for characterizing molecular interactions.
abstract: The field of label-free biophysical technologies used to quantitatively characterize macromolecular interactions with each other and with small molecules has grown enormously in the last 10 years. The most widely used analytical technologies for characterizing biomolecular interactions are surface plasmon resonance (SPR), isothermal titration calorimetry (ITC), biolayer interferometry (BLI), and analytical ultracentrifugation (AUC). Measuring interaction parameters accurately and quantitatively is challenging, as it requires specialized expertise, training, and instrumentation. The Molecular Interaction Research Group (MIRG) conducted an online survey designed to capture the current profile of label-free technologies, including ITC, SPR, and other biosensors used in academia and the pharmaceutical industry sector. The main goal of the survey was to take a snapshot of laboratory, instrumentation, applications for measuring various biophysical parameters, confidence in data interpretation, data validation and acceptability, and limitations of using various technologies. Through this survey, we anticipate that the participating laboratories will be able to gauge their own capabilities and gain insights into the relative success of the different technologies that they use for characterizing molecular interactions.
authors.affiliation: Lerner Research Institute, Cleveland Clinic Foundation, Cleveland, Ohio 44195, USA. yadavs@ccf.org
authors.forename: Satya P
authors.initials: SP
authors.lastname: Yadav
authors.forename: Simon
authors.initials: S
authors.lastname: Bergqvist
authors.forename: Michael L
authors.initials: ML
authors.lastname: Doyle
authors.forename: Thomas A
authors.initials: TA
authors.lastname: Neubert
authors.forename: Aaron P
authors.initials: AP
authors.lastname: Yamniuk
mesh_terms: D002151:Calorimetry / Q000706:statistics & numerical data*; D004345:Drug Industry; D011485:Protein Binding; D025941:Protein Interaction Mapping / Q000706:statistics & numerical data; D020349:Surface Plasmon Resonance / Q000706:statistics & numerical data*; D011795:Surveys and Questionnaires; D013816:Thermodynamics; D017186:Titrimetry