{"response":{"award":[{"abstractText":"The broader impact/commercial potential of this I-Corps project is to explore translation of a sensor for better diagnostics and therapeutics. The proposed technology can be created at low cost, enabling an instrument that integrates parallel sensors for a high-throughput system.\r\n\r\nThis I-Corps project explores applications for the Interferometric Reflectance Imaging Sensor (IRIS), a label-free detection (LFD) system. The proposed system uses optical biosensors in multiplexed imaging detection of molecular binding kinetics on Si-based microfluidic chips as low-cost consumables. Hundreds of capture probes can be arrayed on the IRIS chip and tested against a target molecule in parallel. The proposed system addresses needs for multiplexed and robust small molecule affinity measurements, which can enable the discovery of new ligands for detection and monitoring of small molecules for compact sensors.\r\n\r\nThis award reflects NSF's statutory mission and has been deemed worthy of support through evaluation using the Foundation's intellectual merit and broader impacts review criteria.","activeAwd":"false","agency":"NSF","awardAgencyCode":"4900","awardee":"TRUSTEES OF BOSTON UNIVERSITY","awardeeAddress":"1 SILBER WAY","awardeeCity":"BOSTON","awardeeCountryCode":"US","awardeeDistrict":"07","awardeeDistrictCode":"MA07","awardeeName":"Trustees of Boston University","awardeePhone":"6173534365","awardeeStateCode":"MA","awardeeZipCode":"022151703","cfdaNumber":"47.084","date":"06/10/2020","dirAbbr":"TIP","divAbbr":"TI","estimatedTotalAmt":"50000","expDate":"11/30/2021","fundAgencyCode":"4900","fundProgramName":"I-Corps","fundsObligated":["FY 2020 = $50,000.00"],"fundsObligatedAmt":"50000","histAwd":"false","id":"2027109","initAmendmentDate":"06/10/2020","jrnl":[{"artTitl":"Instrument-Free Protein Microarray Fabrication for Accurate Affinity Measurements","auth":"Celebi, Iris and Geib, Matthew T. and Chiodi, Elisa and Lortlar Ünlü, Nese and Ekiz Kanik, Fulya and Ünlü, Selim","dgtlObjId":"https://doi.org/10.3390/bios10110158","jrnlTitl":"Biosensors","jrnlVol":"10","jrnlYr":"2020","parPblcId":"10233924"},{"artTitl":"Multiplexed Affinity Measurements of Extracellular Vesicles Binding Kinetics","auth":"Chiodi, Elisa and Daaboul, George G. and Marn, Allison M. and Ünlü, M. Selim","dgtlObjId":"https://doi.org/10.3390/s21082634","jrnlTitl":"Sensors","jrnlVol":"21","jrnlYr":"2021","parPblcId":"10233926"},{"artTitl":"The Effects of Three-Dimensional Ligand Immobilization on Kinetic Measurements in Biosensors","auth":"Chiodi, Elisa and Marn, Allison M. and Bakhshpour, Monireh and Lortlar Ünlü, Nese and Ünlü, M. Selim","authIndCode":"N","dgtlObjId":"https://doi.org/10.3390/polym14020241","jrnlTitl":"Polymers","jrnlVol":"14","jrnlYr":"2022","parPblcId":"10321134"},{"artTitl":"Highly Multiplexed Label-Free Imaging Sensor for Accurate Quantification of Small-Molecule Binding Kinetics","auth":"Chiodi, Elisa and Marn, Allison M. and Geib, Matthew T. and Ekiz Kanik, Fulya and Rejman, John and AnKrapp, David and Ünlü, M. 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Selim and Chiari, Marcella","dgtlObjId":"https://doi.org/10.1007/s00216-019-02276-1","jrnlTitl":"Analytical and Bioanalytical Chemistry","jrnlVol":"412","jrnlYr":"2020","parPblcId":"10233922"},{"artTitl":"Bulk-Effect-Free Method for Binding Kinetic Measurements Enabling Small-Molecule Affinity Characterization","auth":"Marn, Allison M. and Chiodi, Elisa and Ünlü, M. Selim","dgtlObjId":"https://doi.org/10.1021/acsomega.0c05994","jrnlTitl":"ACS Omega","jrnlVol":"6","jrnlYr":"2021","parPblcId":"10233873"},{"artTitl":"Multiplexed, High-Sensitivity Measurements of Antibody Affinity Using Interferometric Reflectance Imaging Sensor","auth":"Marn, Allison M. and Needham, James and Chiodi, Elisa and Ünlü, M. Selim","authIndCode":"N","dgtlObjId":"https://doi.org/10.3390/bios11120483","jrnlTitl":"Biosensors","jrnlVol":"11","jrnlYr":"2021","parPblcId":"10321135"}],"latestAmendmentDate":"06/10/2020","managingPec":"802300","orgCodeDir":"15000000","orgCodeDiv":"15030000","orgLongName":"Directorate for Technology, Innovation, and Partnerships","orgLongName2":"Translational Impacts","orgUrl":"https://beta.nsf.gov/tip/ti","parentUeiNumber":"","pdPIName":"Selim Unlu","perfAddress":"8 Saint Marys St","perfCity":"Boston","perfCountryCode":"US","perfDistrict":"07","perfDistrictCode":"MA07","perfLocation":"Trustees of Boston University","perfStateCode":"MA","perfZipCode":"022152421","pi":["Selim Unlu selimunlu@gmail.com"],"piEmail":"selimunlu@gmail.com","piFirstName":"Selim","piId":"000217932","piLastName":"Unlu","poEmail":"rshuman@nsf.gov","poName":"Ruth Shuman","poPhone":"7032922160","primaryProgram":["01002021DB NSF RESEARCH & RELATED ACTIVIT"],"progEleCode":"802300","program":"","progRefCode":"","projectOutComesReport":"
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Synergistic collaboration of researchers from multiple disciplines of science and engineering has been crucial for advances in understanding biomolecular interactions.  Since all biological pathways rely on protein-DNA, protein-protein, and other biomolecular interactions, not only is accurate characterization of these interactions crucial, but also, they are prime targets for disruption with small molecules in disease treatment. Both in vitro diagnostics (IVD) and pharmaceutical industry rely on biotechnology tools to discover and develop new molecular interactions.  There is an increasing demand to measure the affinities of biomarkers both for new medicines and diagnostics. The IVD and pharma industries are growing robustly. To address emerging market and technical challenges, industry needs a robust, quantitative, and high-sensitivity label-free technology for accurate analysis binding kinetics of biomolecules from proteins to small molecule analytes.

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 The customers? need for better understanding of binding kinetics using native proteins and ligands is the driving motivation for molecular kinetics by Label Free Detection (LFD).  Many LFD techniques rely on non-linear and complex dependence of transduced signal on the molecular binding to increase sensitivity yielding signals difficult to decode and quantify, and often, LFD is regarded as a \"black box\" technology. Our innovation - Interferometric Reflectance Imaging Sensor, iRiS - defies the conventional wisdom that calls for enhancing the signal through complex optical resonances. Instead, we exploit light interference from an optically transparent thin film?the same phenomenon that gives rainbow colors to a soap film when illuminated by white light.

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iRiS Kinetics (Team 1814) participated in the first remote cohort of I-CORPS training program. Through the program, we have conducted 103 interviews (81 video, 22 phone) and refined the value proposition for the label-free molecular binding kinetics reader. We concluded that \"Principal Investigators in academic labs will buy IRIS multiplexed affinity reader to study molecular kinetics because they can get access to publication-quality kinetic data from their own bench.\" 

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This effort has also been supported by an NSF Technology Translation Award and a Boston University Ignition Award. These grants enabled the demonstration of technical performance of the multiplexed reader. We have published a number of journal articles demonstrating the superior performance of iRiS technology. We have built a Minimum Viable Product (MVP) and received invaluable feedback. Finally, a start-up company (iriskinetics.com) has been successfully launched. 


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\n\t\t\t\t \tLast Modified: 04/08/2022
\n\t\t\t\t\tModified by: M. Selim Unlu

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  • \n\"Team\n
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    We zoom'ed all over the world as part of the first remote cohort of I-CORPS program
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    Elisa Chiodi - Allison Marn
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    Public Domain
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    M. Selim Unlu
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    Team iRiS interviews
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  • \n\"AACC\n
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    Iris Celebi and Elisa Chiodi presenting a poster on iRiS Technology
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    Selim �nl�
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    M. Selim Unlu
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","publicAccessMandate":"1","publicationResearch":["Biosensors~2020~10~Celebi, Iris and Geib, Matthew T. and Chiodi, Elisa and Lortlar Ünlü, Nese and Ekiz Kanik, Fulya and Ünlü, Selim~https://doi.org/10.3390/bios10110158~Instrument-Free Protein Microarray Fabrication for Accurate Affinity Measurements~158~10233924~10233924~OSTI~2021-06-02 21:03:31.963","Sensors~2021~21~Chiodi, Elisa and Daaboul, George G. and Marn, Allison M. and Ünlü, M. Selim~https://doi.org/10.3390/s21082634~Multiplexed Affinity Measurements of Extracellular Vesicles Binding Kinetics~2634~10233926~10233926~OSTI~2021-06-02 21:03:26.013","Polymers~2022~14~Chiodi, Elisa and Marn, Allison M. and Bakhshpour, Monireh and Lortlar Ünlü, Nese and Ünlü, M. Selim~https://doi.org/10.3390/polym14020241~The Effects of Three-Dimensional Ligand Immobilization on Kinetic Measurements in Biosensors~N~10321134~10321134~OSTI~2023-03-13 01:34:37.843","ACS Omega~2020~5~Chiodi, Elisa and Marn, Allison M. and Geib, Matthew T. and Ekiz Kanik, Fulya and Rejman, John and AnKrapp, David and Ünlü, M. Selim~https://doi.org/10.1021/acsomega.0c03708~Highly Multiplexed Label-Free Imaging Sensor for Accurate Quantification of Small-Molecule Binding Kinetics~25358 to 25364~10233876~10233876~OSTI~2021-06-02 21:03:32.773","Polymers~2021~13~Chiodi, Elisa and Marn, Allison M. and Geib, Matthew T. and Ünlü, M. Selim~https://doi.org/10.3390/polym13071026~The Role of Surface Chemistry in the Efficacy of Protein and DNA Microarrays for Label-Free Detection: An Overview~1026~10233927~10233927~OSTI~2021-06-03 01:03:29.01","Analytical and Bioanalytical Chemistry~2020~412~Chiodi, Elisa and Sola, Laura and Brambilla, Dario and Cretich, Marina and Marn, Allison Marie and Ünlü, M. Selim and Chiari, Marcella~https://doi.org/10.1007/s00216-019-02276-1~Simultaneous evaluation of multiple microarray surface chemistries through real-time interferometric imaging~3477 to 3487~10233922~10233922~OSTI~2021-06-02 21:03:35.736","ACS Omega~2021~6~Marn, Allison M. and Chiodi, Elisa and Ünlü, M. Selim~https://doi.org/10.1021/acsomega.0c05994~Bulk-Effect-Free Method for Binding Kinetic Measurements Enabling Small-Molecule Affinity Characterization~6836 to 6841~10233873~10233873~OSTI~2021-06-02 21:03:26.636","Biosensors~2021~11~Marn, Allison M. and Needham, James and Chiodi, Elisa and Ünlü, M. Selim~https://doi.org/10.3390/bios11120483~Multiplexed, High-Sensitivity Measurements of Antibody Affinity Using Interferometric Reflectance Imaging Sensor~N~10321135~10321135~OSTI~2022-04-08 17:03:14.79"],"startDate":"06/01/2020","title":"I-Corps: Interferometric Imaging for Multiplexed Molecular Kinetics","transType":"Standard Grant","ueiNumber":"THL6A6JLE1S7"}],"metadata":{"offset":0,"rpp":25,"totalCount":1}}}