Bio-layer interferometry: Difference between revisions
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[[File:Bio-layer interferometry without analyte binding.gif|thumb| |
[[File:Bio-layer interferometry without analyte binding.gif|thumb|Overview schematic of a Bio-layer interferometry setup]] |
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[[File:Bio-layer interferometry with analyte binding.gif|thumb|Figure 2]] |
[[File:Bio-layer interferometry with analyte binding.gif|thumb|Figure 2]] |
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[[File:Bio-layer interferometry wavelength shift due to analyte binding.gif|thumb|Figure 3]] |
[[File:Bio-layer interferometry wavelength shift due to analyte binding.gif|thumb|Figure 3]] |
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'''Bio-layer interferometry (BLI)''' is a modern biosensing technology that analyzes biomolecular interactions in real-time without the need for fluorescent labeling.<ref>{{Cite book|last=David.|first=Apiyo,|url=http://worldcat.org/oclc/988866146|title=Handbook of Surface Plasmon Resonance.|date=2017|publisher=Royal Society of Chemistry|isbn=978-1-78801-139-6|oclc=988866146}}</ref> Alongside [[Surface plasmon resonance|Surface Plasmon Resonance]], BLI is one of few widely available [[Label-free quantification|label-free]] biosensing technologies, a detection style that allows for a higher volume of information to be obtained in a quicker amount of time compared to traditional processes.<ref>{{Cite journal|last=Syahir|first=Amir|last2=Usui|first2=Kenji|last3=Tomizaki|first3=Kin-ya|last4=Kajikawa|first4=Kotaro|last5=Mihara|first5=Hisakazu|date=2015-04-24|title=Label and Label-Free Detection Techniques for Protein Microarrays|url=http://dx.doi.org/10.3390/microarrays4020228|journal=Microarrays|volume=4|issue=2|pages=228–244|doi=10.3390/microarrays4020228|issn=2076-3905}}</ref> The technology relies on the phase shift-wavelength correlation created between interference patterns off of two unique surfaces on the tip of a biosensor.<ref>{{Cite journal|last=Müller-Esparza|first=Hanna|last2=Osorio-Valeriano|first2=Manuel|last3=Steube|first3=Niklas|last4=Thanbichler|first4=Martin|last5=Randau|first5=Lennart|date=2020-05-27|title=Bio-Layer Interferometry Analysis of the Target Binding Activity of CRISPR-Cas Effector Complexes|url=http://dx.doi.org/10.3389/fmolb.2020.00098|journal=Frontiers in Molecular Biosciences|volume=7|doi=10.3389/fmolb.2020.00098|issn=2296-889X}}</ref> BLI has significant applications in quantifying binding strength, measuring protein interactions, and identifying properties of reaction kinetics, such as rate constants and reaction rates.<ref>{{cite journal|last1=Rich|first1=Rebecca L|last2=Myszka|first2=David G|date=1 February 2007|title=Higher-throughput, label-free, real-time molecular interaction analysis.|journal=Analytical Biochemistry|volume=361|issue=1|pages=1–6|doi=10.1016/j.ab.2006.10.040|pmid=17145039}}</ref> |
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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). |
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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=2|location=Cambridge, England|oclc=1012492391}}</ref> |
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=2|location=Cambridge, England|oclc=1012492391}}</ref> |
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Revision as of 00:28, 14 November 2021
Bio-layer interferometry (BLI) is a modern biosensing technology that analyzes biomolecular interactions in real-time without the need for fluorescent labeling.[1] Alongside Surface Plasmon Resonance, BLI is one of few widely available label-free biosensing technologies, a detection style that allows for a higher volume of information to be obtained in a quicker amount of time compared to traditional processes.[2] The technology relies on the phase shift-wavelength correlation created between interference patterns off of two unique surfaces on the tip of a biosensor.[3] BLI has significant applications in quantifying binding strength, measuring protein interactions, and identifying properties of reaction kinetics, such as rate constants and reaction rates.[4]
The binding between a 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.[5]
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,[6] quantitation, affinity,[7] and kinetics.[8]
Bio-layer interferometry was pioneered by the founders of FortéBio, an instrument manufacturer based in Fremont, California. In 2011, FortéBio was acquired by Pall Corporation. After Danaher's acquisition of Pall, FortéBio remained under Pall until 2018. Between 2018 and 2020, FortéBio was a business unit of Molecular Devices.[9] In April 2020, FortéBio was acquired by Sartorius.[10]
References
- ^ David., Apiyo, (2017). Handbook of Surface Plasmon Resonance. Royal Society of Chemistry. ISBN 978-1-78801-139-6. OCLC 988866146.
{{cite book}}: CS1 maint: extra punctuation (link) CS1 maint: multiple names: authors list (link) - ^ Syahir, Amir; Usui, Kenji; Tomizaki, Kin-ya; Kajikawa, Kotaro; Mihara, Hisakazu (2015-04-24). "Label and Label-Free Detection Techniques for Protein Microarrays". Microarrays. 4 (2): 228–244. doi:10.3390/microarrays4020228. ISSN 2076-3905.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - ^ Müller-Esparza, Hanna; Osorio-Valeriano, Manuel; Steube, Niklas; Thanbichler, Martin; Randau, Lennart (2020-05-27). "Bio-Layer Interferometry Analysis of the Target Binding Activity of CRISPR-Cas Effector Complexes". Frontiers in Molecular Biosciences. 7. doi:10.3389/fmolb.2020.00098. ISSN 2296-889X.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - ^ Rich, Rebecca L; Myszka, David G (1 February 2007). "Higher-throughput, label-free, real-time molecular interaction analysis". Analytical Biochemistry. 361 (1): 1–6. doi:10.1016/j.ab.2006.10.040. PMID 17145039.
- ^ Handbook of surface plasmon resonance. R. B. M. Schasfoort (2 ed.). Cambridge, England. 2017. ISBN 978-1-78801-028-3. OCLC 1012492391.
{{cite book}}: CS1 maint: location missing publisher (link) CS1 maint: others (link) - ^ Fang, Ye (20 November 2006). "Label-Free Cell-Based Assays with Optical Biosensors in Drug Discovery". Assay and Drug Development Technologies. 4 (5): 583–595. doi:10.1089/adt.2006.4.583. PMID 17115929.
- ^ Fransson, Johan; Teplyakov, Alexey; Raghunathan, Gopalan; Chi, Ellen; Cordier, Wendy; Dinh, Thai; Feng, Yiqing; Giles-Komar, Jill; Gilliland, Gary; Lollo, Bridget; Malia, Thomas J; Nishioka, Walter; Obmolova, Galina; Zhao, Shanrong; Zhao, Yonghong; Swanson, Ronald V; Almagro, Juan C (30 April 2010). "Human Framework Adaptation of a Mouse Anti-Human IL-13 Antibody". Journal of Molecular Biology. 398 (2): 214–231. doi:10.1016/j.jmb.2010.03.004. PMID 20226193.
- ^ Abdiche, Yasmina; Malashock, Dan; Pinkerton, Alanna; Pons, Jaume (15 June 2008). "Determining kinetics and affinities of protein interactions using a parallel real-time label-free biosensor, the Octet". Analytical Biochemistry. 377 (2): 209–217. doi:10.1016/j.ab.2008.03.035. PMID 18405656.
- ^ "Molecular Devices announces brand identity for its newly-formed biologics business unit". www.fortebio.com. Retrieved 24 November 2018.
- ^ "News Releases | ForteBio". www.fortebio.com. Retrieved 2020-06-08.