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'''Bio-layer interferometry''' ('''BLI''') is a [[label-free_quantification|label-free]] technology for measuring [[molecular interaction|biomolecular interactions]].<ref>{{cite journal |last1=Cooper |first1=Matthew |title=Current biosensor technologies in drug discovery. |journal=Drug Discovery World |date=May 7, 2006 |issue=Summer |pages=68–82 |url=https://www.ddw-online.com/drug-discovery/p97058-current-biosensor-technologies-in-drug-discoverysummer-06.html}}</ref><ref>{{cite journal |last1=Rich |first1=Rebecca L |last2=Myszka |first2=David G |title=Higher-throughput, label-free, real-time molecular interaction analysis. |journal=Analytical Biochemistry |date=1 February 2007 |volume=361 |issue=1 |pages=1–6 |doi=10.1016/j.ab.2006.10.040 |pmid=17145039 }}</ref> It is an optical analytical technique that analyzes the [[Interference (wave propagation)|interference]] pattern of white light reflected from two surfaces: a layer of immobilized [[protein]] on the biosensor tip, and an internal reference layer (Figure 1). Any change in the number of molecules bound to the biosensor tip causes a shift in the interference pattern that can be measured in real-time (Figures 1 and 2).
The binding between a [[Ligand (biochemistry)|ligand]] immobilized on the biosensor tip surface and an analyte in solution produces an increase in [[optical thickness]] at the biosensor tip, which results in a [[wavelength]] shift, Δλ (Figure 3), which is a direct measure of the change in thickness of the biological layer. Interactions are measured in real time, providing the ability to monitor binding specificity, rates of association and dissociation, or concentration, with high precision and accuracy.<ref>{{Cite book|url=https://www.worldcat.org/oclc/1012492391|title=Handbook of surface plasmon resonance|date=2017|others=R. B. M. Schasfoort|isbn=978-1-78801-028-3|edition=2nd edition|___location=Cambridge, England|oclc=1012492391}}</ref>
Only molecules binding to or dissociating from the biosensor can shift the interference pattern and generate a response profile. Unbound molecules, changes in the [[refractive index]] of the surrounding medium, or changes in flow rate do not affect the interference pattern. This is a unique characteristic of bio-layer interferometry and extends its capability to perform in crude samples used in applications for protein-protein interactions,<ref>{{cite journal |last1=Fang |first1=Ye |title=Label-Free Cell-Based Assays with Optical Biosensors in Drug Discovery |journal=Assay and Drug Development Technologies |date=20 November 2006 |volume=4 |issue=5 |pages=583–595 |doi=10.1089/adt.2006.4.583 |pmid=17115929 }}</ref> quantitation, affinity,<ref>{{cite journal |last1=Fransson |first1=Johan |last2=Teplyakov |first2=Alexey |last3=Raghunathan |first3=Gopalan |last4=Chi |first4=Ellen |last5=Cordier |first5=Wendy |last6=Dinh |first6=Thai |last7=Feng |first7=Yiqing |last8=Giles-Komar |first8=Jill |last9=Gilliland |first9=Gary |last10=Lollo |first10=Bridget |last11=Malia |first11=Thomas J |last12=Nishioka |first12=Walter |last13=Obmolova |first13=Galina |last14=Zhao |first14=Shanrong |last15=Zhao |first15=Yonghong |last16=Swanson |first16=Ronald V |last17=Almagro |first17=Juan C |title=Human Framework Adaptation of a Mouse Anti-Human IL-13 Antibody |journal=Journal of Molecular Biology |date=30 April 2010 |volume=398 |issue=2 |pages=214–231 |doi=10.1016/j.jmb.2010.03.004 |pmid=20226193 }}</ref> and kinetics.<ref>{{cite journal |last1=Abdiche |first1=Yasmina |last2=Malashock |first2=Dan |last3=Pinkerton |first3=Alanna |last4=Pons |first4=Jaume |title=Determining kinetics and affinities of protein interactions using a parallel real-time label-free biosensor, the Octet |journal=Analytical Biochemistry |date=15 June 2008 |volume=377 |issue=2 |pages=209–217 |doi=10.1016/j.ab.2008.03.035 |pmid=18405656 }}</ref>
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