{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,11,11]],"date-time":"2025-11-11T13:08:41Z","timestamp":1762866521962,"version":"build-2065373602"},"reference-count":39,"publisher":"MDPI AG","issue":"12","license":[{"start":{"date-parts":[[2014,12,5]],"date-time":"2014-12-05T00:00:00Z","timestamp":1417737600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Taiwan NSC","award":["101-2112-M-030-003-MY3"],"award-info":[{"award-number":["101-2112-M-030-003-MY3"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Sensors"],"abstract":"<jats:p>One of the most important goals in proteomics is to detect the real-time kinetics of diverse biomolecular interactions. Fluorescence, which requires extrinsic tags, is a commonly and widely used method because of its high convenience and sensitivity. However, in order to maintain the conformational and functional integrality of biomolecules, label-free detection methods are highly under demand. We have developed the oblique-incidence reflectivity difference (OI-RD) technique for label-free, kinetic measurements of protein-biomolecule interactions. Incorporating the total internal refection geometry into the OI-RD technique, we are able to detect as low as 0.1% of a protein monolayer, and this sensitivity is comparable with other label-free techniques such as surface plasmon resonance (SPR). The unique advantage of OI-RD over SPR is no need for dielectric layers. Moreover, using a photodiode array as the detector enables  multi-channel detection and also eliminates the over-time signal drift. In this paper, we demonstrate the applicability and feasibility of the OI-RD technique by measuring the kinetics of protein-protein and protein-small molecule interactions in sandwich assays.<\/jats:p>","DOI":"10.3390\/s141223307","type":"journal-article","created":{"date-parts":[[2014,12,5]],"date-time":"2014-12-05T10:20:05Z","timestamp":1417774805000},"page":"23307-23320","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Real-Time, Label-Free Detection of Biomolecular Interactions in Sandwich Assays by the Oblique-Incidence Reflectivity  Difference Technique"],"prefix":"10.3390","volume":"14","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-7513-0251","authenticated-orcid":false,"given":"Yung-Shin","family":"Sun","sequence":"first","affiliation":[{"name":"Department of Physics, Fu-Jen Catholic University, New Taipei City 24205, Taiwan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Xiangdong","family":"Zhu","sequence":"additional","affiliation":[{"name":"Department of Physics, University of California at Davis, Davis, CA 95616, USA"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2014,12,5]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"1156","DOI":"10.1021\/ac970805y","article-title":"Regenerable biosensor platform: A total internal reflection fluorescence cell with electrochemical control","volume":"70","author":"Asanov","year":"1998","journal-title":"Anal. 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