Method for estimating the single molecular affinity
Affinity constants (kd, ka, and KD) can be determined by methods that apply immobilized ligands such as immunoassays and label-free biosensor technologies. This article outlines a new surface plasmon resonance (SPR) array imaging method that yields affinity constants that can be considered as the be...
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| Veröffentlicht in: | Analytical biochemistry 2012-02, Vol.421 (2), p.794-796 |
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| container_issue | 2 |
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| container_title | Analytical biochemistry |
| container_volume | 421 |
| creator | Schasfoort, Richard B.M. de Lau, Wim van der Kooi, Alex Clevers, Hans Engbers, Gerard H.M. |
| description | Affinity constants (kd, ka, and KD) can be determined by methods that apply immobilized ligands such as immunoassays and label-free biosensor technologies. This article outlines a new surface plasmon resonance (SPR) array imaging method that yields affinity constants that can be considered as the best estimate of the affinity constant for single biomolecular interactions. Calculated rate (kd and ka) and dissociation equilibrium (KD) constants for various ligand densities and analyte concentrations are extrapolated to the KD at the zero response level (KDR0). By applying this method to an LGR5-exo-Fc–RSPO1-FH interaction couple, the KDR0 was determined as 3.1nM. |
| doi_str_mv | 10.1016/j.ab.2011.12.011 |
| format | Article |
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By applying this method to an LGR5-exo-Fc–RSPO1-FH interaction couple, the KDR0 was determined as 3.1nM.</description><subject>biosensors</subject><subject>dissociation</subject><subject>image analysis</subject><subject>immunoassays</subject><subject>Kinetics</subject><subject>Label free</subject><subject>Ligands</subject><subject>Protein Array Analysis</subject><subject>Protein interaction analysis</subject><subject>Protein Interaction Maps</subject><subject>Rate and dissociation equilibrium constants</subject><subject>SPR imaging</subject><subject>Surface Plasmon Resonance</subject><subject>yields</subject><issn>0003-2697</issn><issn>1096-0309</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kD1PwzAQhi0EoqWwM0E2poTzR9yEDVV8SUUM0NlynHPrKmnATpD673HVwsb0enjuPd9DyCWFjAKVt-tMVxkDSjPKshhHZEyhlClwKI_JGAB4ymQ5HZGzENYQCZHLUzJijEE55XJM-Cv2q65ObOcTDL1rde82y6RfYRLio8Gk7Ro0Q6N9oq11G9dvz8mJ1U3Ai0NOyOLx4WP2nM7fnl5m9_PUCJr3aS1lURQVp8ZUWlDNatBFXnNupc7RiMLmohIGSpCUCSsoMhSFqIuqEmW8gk_Izb7303dfQ_ydal0w2DR6g90QVMmA73ZMIwl70vguBI9Wffp4it8qCmpnSq2VrtTOlKJMxYgjV4fyoWqx_hv4VROB6z1gdaf00rugFu-xQUartKD5ruJuT2CU8O3Qq2AcbgzWzqPpVd25__f_AJNDf8o</recordid><startdate>20120215</startdate><enddate>20120215</enddate><creator>Schasfoort, Richard B.M.</creator><creator>de Lau, Wim</creator><creator>van der Kooi, Alex</creator><creator>Clevers, Hans</creator><creator>Engbers, Gerard H.M.</creator><general>Elsevier Inc</general><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20120215</creationdate><title>Method for estimating the single molecular affinity</title><author>Schasfoort, Richard B.M. ; de Lau, Wim ; van der Kooi, Alex ; Clevers, Hans ; Engbers, Gerard H.M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c415t-d66888b31ccba41a2d0a85d33f6a5ec48f54b4c0906124f41e2e484d8bb490963</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>biosensors</topic><topic>dissociation</topic><topic>image analysis</topic><topic>immunoassays</topic><topic>Kinetics</topic><topic>Label free</topic><topic>Ligands</topic><topic>Protein Array Analysis</topic><topic>Protein interaction analysis</topic><topic>Protein Interaction Maps</topic><topic>Rate and dissociation equilibrium constants</topic><topic>SPR imaging</topic><topic>Surface Plasmon Resonance</topic><topic>yields</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Schasfoort, Richard B.M.</creatorcontrib><creatorcontrib>de Lau, Wim</creatorcontrib><creatorcontrib>van der Kooi, Alex</creatorcontrib><creatorcontrib>Clevers, Hans</creatorcontrib><creatorcontrib>Engbers, Gerard H.M.</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Analytical biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Schasfoort, Richard B.M.</au><au>de Lau, Wim</au><au>van der Kooi, Alex</au><au>Clevers, Hans</au><au>Engbers, Gerard H.M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Method for estimating the single molecular affinity</atitle><jtitle>Analytical biochemistry</jtitle><addtitle>Anal Biochem</addtitle><date>2012-02-15</date><risdate>2012</risdate><volume>421</volume><issue>2</issue><spage>794</spage><epage>796</epage><pages>794-796</pages><issn>0003-2697</issn><eissn>1096-0309</eissn><abstract>Affinity constants (kd, ka, and KD) can be determined by methods that apply immobilized ligands such as immunoassays and label-free biosensor technologies. 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| ispartof | Analytical biochemistry, 2012-02, Vol.421 (2), p.794-796 |
| issn | 0003-2697 1096-0309 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | biosensors dissociation image analysis immunoassays Kinetics Label free Ligands Protein Array Analysis Protein interaction analysis Protein Interaction Maps Rate and dissociation equilibrium constants SPR imaging Surface Plasmon Resonance yields |
| title | Method for estimating the single molecular affinity |
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