Bio-layer interferometry: Difference between revisions

Revision as of 12:26, 5 June 2023

Revision as of 17:29, 14 December 2023

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=== Biosensor Type and Selection ===

Bio-layer interferometry relies on [[Biosensor|biosensors]] with a fiber optic tip upon which the ligand is immobilized.<ref name="Apiyo_2017" /> The tip is additionally coated with a matrix biocompatible with the target molecule to limit any non-specific binding. For BLI calculations to work, it is necessary to assume that both the fiber optic tip and the bound ligand and analyte act as thin, reflective surfaces.<ref>{{Cite journal| vauthors = Gao S, Zheng X, Wu J |date=2017|title=A biolayer interferometry-based competitive biosensor for rapid and sensitive detection of saxitoxin |journal=Sensors and Actuators B: Chemical|volume=246|pages=169–174|doi=10.1016/j.snb.2017.02.078|issn=0925-4005}}</ref> The biosensors are disposable, resulting in low costs and high commercial availability.<ref>{{cite journal | vauthors = Abdiche Y, Malashock D, Pinkerton A, Pons J | title = Determining kinetics and affinities of protein interactions using a parallel real-time label-free biosensor, the Octet | journal = Analytical Biochemistry | volume = 377 | issue = 2 | pages = 209–217 | date = June 2008 | pmid = 18405656 | doi = 10.1016/j.ab.2008.03.035 | doi-access = free }}</ref> Biosensor selection is determined by the desired test results: kinetic analysis, quantitative analysis, or both.<ref>{{cite journal | vauthors = Yu Y, Mitchell S, Lynaugh H, Brown M, Nobrega RP, Zhi X, Sun T, Caffry I, Cao Y, Yang R, Burnina I, Xu Y, Estep P | display-authors = 6 | title = Understanding ForteBio's Sensors for High-Throughput Kinetic and Epitope Screening for Purified Antibodies and Yeast Culture Supernatant | journal = Journal of Biomolecular Screening | volume = 21 | issue = 1 | pages = 88–95 | date = January 2016 | pmid = 26442912 | doi = 10.1177/1087057115609564 | pmc = 4708621 | doi-access = free }}</ref> Most commercially available biosensor types will be grouped into one of these three categories by the BLI manufacturer.<ref name="Apiyo_2017" />

== Applications ==

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== Distinguishing Characteristics ==

BLI and SPR are both dominant technologies in the label-free instruments market.<ref name="Apiyo_2017" /> Despite sharing some similarities in concept, there are significant differences between the two techniques. Micro-fluidic SPR relies on a closed architecture to transport samples to a stationary sensor chip (Figure 4). BLI instead utilizes an open system, shaking multiple wells on a plate to transport the sensors to the samples without need for [[Microfluidics|micro-fluidics]].<ref name=":2">{{cite journal | vauthors = Wallner J, Lhota G, Jeschek D, Mader A, Vorauer-Uhl K | title = Application of Bio-Layer Interferometry for the analysis of protein/liposome interactions | journal = Journal of Pharmaceutical and Biomedical Analysis | volume = 72 | pages = 150–154 | date = January 2013 | pmid = 23146240 | doi = 10.1016/j.jpba.2012.10.008 }}</ref> Being a closed system, SPR's association and dissociation phases are limited by the technology's design. BLI's open plate design results in association and dissociation length limits determined by sample evaporation instead.<ref>{{cite journal | vauthors = Abdiche Y, Malashock D, Pinkerton A, Pons J | title = Determining kinetics and affinities of protein interactions using a parallel real-time label-free biosensor, the Octet | journal = Analytical Biochemistry | volume = 377 | issue = 2 | pages = 209–217 | date = June 2008 | pmid = 18405656 | doi = 10.1016/j.ab.2008.03.035 | doi-access = free }}</ref> SPR is easily reproducible due to its continuous flow microfluidics. BLI's multi well plate design allows for extremely high throughput in one batch. [[Assay]] configuration in BLI can, in stable conditions, allow for recovery of samples. Assay configuration in SPR allows for higher sensitivity. As a result, BLI results are often compared to SPR results for validation.<ref>{{cite journal | vauthors = Yang D, Singh A, Wu H, Kroe-Barrett R | title = Comparison of biosensor platforms in the evaluation of high affinity antibody-antigen binding kinetics | journal = Analytical Biochemistry | volume = 508 | pages = 78–96 | date = September 2016 | pmid = 27365220 | doi = 10.1016/j.ab.2016.06.024 | doi-access = free }}</ref>

== References ==

{{Reflist|2}}