{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,4]],"date-time":"2026-07-04T01:41:27Z","timestamp":1783129287025,"version":"3.54.6"},"reference-count":17,"publisher":"Wiley","issue":"22","license":[{"start":{"date-parts":[[2010,10,22]],"date-time":"2010-10-22T00:00:00Z","timestamp":1287705600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Electrophoresis"],"published-print":{"date-parts":[[2010,11]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Back\u2010scattering interferometry (BSI) is a label\u2010free, free\u2010solution, small\u2010volume technique used for characterizing binding interactions, which is also relevant to a growing number of biosensing applications including drug discovery. Here, we use BSI to characterize the interaction of carbonic anhydrase enzyme II with five well\u2010known carbonic anhydrase enzyme II inhibitors (\u00b1sulpiride, sulfanilamide, benzene sulfonamide, dansylamide, and acetazolamide) in the presence of DMSO. Dissociation constants calculated for each interaction were consistent with literature values previously obtained using surface plasmon resonance and fluorescence\u2010based competition assays. Results demonstrate the potential of BSI as a drug\u2010screening tool which is fully compatible with DMSO and does not require immobilization or labeling, therefore allowing binding interactions to be characterized in the native state. BSI has the potential for reducing labor costs, sample consumption, and assay time while providing enhanced reliability over existing techniques.<\/jats:p>","DOI":"10.1002\/elps.201000389","type":"journal-article","created":{"date-parts":[[2010,10,22]],"date-time":"2010-10-22T06:42:04Z","timestamp":1287729724000},"page":"3691-3695","source":"Crossref","is-referenced-by-count":16,"title":["Free\u2010solution interaction assay of carbonic anhydrase to its inhibitors using back\u2010scattering interferometry"],"prefix":"10.1002","volume":"31","author":[{"given":"Ereny F.","family":"Morcos","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Amanda","family":"Kussrow","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carolyn","family":"Enders","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Darryl","family":"Bornhop","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2010,10,22]]},"reference":[{"key":"e_1_2_3_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.drudis.2006.10.003"},{"key":"e_1_2_3_3_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.aca.2008.05.022"},{"key":"e_1_2_3_4_2","doi-asserted-by":"publisher","DOI":"10.1007\/s00216-009-2637-8"},{"key":"e_1_2_3_5_2","doi-asserted-by":"publisher","DOI":"10.1021\/ac051802l"},{"key":"e_1_2_3_6_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.1146559"},{"key":"e_1_2_3_7_2","doi-asserted-by":"publisher","DOI":"10.1002\/jmr.1025"},{"key":"e_1_2_3_8_2","doi-asserted-by":"crossref","first-page":"F110","DOI":"10.1152\/ajpcell.1983.245.5.C334","volume":"245","author":"Brown D.","year":"1983","journal-title":"Am. 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