{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,9,23]],"date-time":"2025-09-23T13:47:32Z","timestamp":1758635252021},"reference-count":50,"publisher":"Wiley","license":[{"start":{"date-parts":[[2016,1,1]],"date-time":"2016-01-01T00:00:00Z","timestamp":1451606400000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal of Sensors"],"published-print":{"date-parts":[[2016]]},"abstract":"<jats:p>Efficient biorecognition of thrombin (TB), a serine protease with crucial role in physiological and pathological blood coagulation, is a hot topic in medical diagnostics. In this work, we investigate the ability of synthetic thrombin aptamer (TBA), immobilized on a gold substrate, to bind thrombin by two different label-free techniques: the quartz crystal microbalance (QCM) and the spectroscopic ellipsometry (SE). By QCM characterization in the range from 20 to 110\u2009nM, we demonstrate high specificity of TBA-TB interaction and determine affinity constant (<mml:math xmlns:mml=\"http:\/\/www.w3.org\/1998\/Math\/MathML\" id=\"M1\"><mml:mrow><mml:msub><mml:mrow><mml:mi>K<\/mml:mi><\/mml:mrow><mml:mrow><mml:mi>d<\/mml:mi><\/mml:mrow><\/mml:msub><\/mml:mrow><\/mml:math>) of<mml:math xmlns:mml=\"http:\/\/www.w3.org\/1998\/Math\/MathML\" id=\"M2\"><mml:mn fontstyle=\"italic\">17.7<\/mml:mn><mml:mo>\u00b1<\/mml:mo><mml:mn fontstyle=\"italic\">0.3<\/mml:mn><\/mml:math>\u2009nM, system sensitivity of<mml:math xmlns:mml=\"http:\/\/www.w3.org\/1998\/Math\/MathML\" id=\"M3\"><mml:mn fontstyle=\"italic\">0.42<\/mml:mn><mml:mo>\u00b1<\/mml:mo><mml:mn fontstyle=\"italic\">0.03<\/mml:mn><\/mml:math>\u2009Hz\u2009nM<jats:sup>\u22121<\/jats:sup>, and limit of detection (LOD) of<mml:math xmlns:mml=\"http:\/\/www.w3.org\/1998\/Math\/MathML\" id=\"M4\"><mml:mn fontstyle=\"italic\">240<\/mml:mn><mml:mo>\u00b1<\/mml:mo><mml:mn fontstyle=\"italic\">20<\/mml:mn><\/mml:math>\u2009pM. The interaction between TBA and TB is also investigated by SE, an all-optical method, by quantifying the thickness increase of the TBA film assembled on gold substrate. AFM characterization of TBA and TB molecules deposited on flat silicon surface is also supplied.<\/jats:p>","DOI":"10.1155\/2016\/3561863","type":"journal-article","created":{"date-parts":[[2016,5,9]],"date-time":"2016-05-09T21:03:06Z","timestamp":1462827786000},"page":"1-8","source":"Crossref","is-referenced-by-count":8,"title":["Nanogravimetric and Optical Characterizations of Thrombin Interaction with a Self-Assembled Thiolated Aptamer"],"prefix":"10.1155","volume":"2016","author":[{"given":"Jane","family":"Politi","sequence":"first","affiliation":[{"name":"Institute for Microelectronics and Microsystems, National Research Council, Unit of Naples, Via P. 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