Kinetic titration series with biolayer interferometry
Biolayer interferometry is a method to analyze protein interactions in real-time. In this study, we illustrate the usefulness to quantitatively analyze high affinity protein ligand interactions employing a kinetic titration series for characterizing the interactions between two pairs of interaction...
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description | Biolayer interferometry is a method to analyze protein interactions in real-time. In this study, we illustrate the usefulness to quantitatively analyze high affinity protein ligand interactions employing a kinetic titration series for characterizing the interactions between two pairs of interaction patterns, in particular immunoglobulin G and protein G B1 as well as scFv IC16 and amyloid beta (1-42). Kinetic titration series are commonly used in surface plasmon resonance and involve sequential injections of analyte over a desired concentration range on a single ligand coated sensor chip without waiting for complete dissociation between the injections. We show that applying this method to biolayer interferometry is straightforward and i) circumvents problems in data evaluation caused by unavoidable sensor differences, ii) saves resources and iii) increases throughput if screening a multitude of different analyte/ligand combinations. |
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In this study, we illustrate the usefulness to quantitatively analyze high affinity protein ligand interactions employing a kinetic titration series for characterizing the interactions between two pairs of interaction patterns, in particular immunoglobulin G and protein G B1 as well as scFv IC16 and amyloid beta (1-42). Kinetic titration series are commonly used in surface plasmon resonance and involve sequential injections of analyte over a desired concentration range on a single ligand coated sensor chip without waiting for complete dissociation between the injections. We show that applying this method to biolayer interferometry is straightforward and i) circumvents problems in data evaluation caused by unavoidable sensor differences, ii) saves resources and iii) increases throughput if screening a multitude of different analyte/ligand combinations.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0106882</identifier><identifier>PMID: 25229647</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Biochemistry ; Biology and Life Sciences ; Biosensors ; Data analysis ; Design ; Dissociation ; Experiments ; Exports ; Immunoglobulin G ; Immunoglobulins ; Interferometry ; Interferometry - methods ; Kinetics ; Ligands ; Medicine and Health Sciences ; Physical Sciences ; Protein Binding ; Protein G ; Protein interaction ; Proteins ; Sensors ; Surface Plasmon Resonance ; Titration</subject><ispartof>PloS one, 2014-09, Vol.9 (9), p.e106882-e106882</ispartof><rights>2014 Frenzel, Willbold. This is an open-access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. 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In this study, we illustrate the usefulness to quantitatively analyze high affinity protein ligand interactions employing a kinetic titration series for characterizing the interactions between two pairs of interaction patterns, in particular immunoglobulin G and protein G B1 as well as scFv IC16 and amyloid beta (1-42). Kinetic titration series are commonly used in surface plasmon resonance and involve sequential injections of analyte over a desired concentration range on a single ligand coated sensor chip without waiting for complete dissociation between the injections. 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In this study, we illustrate the usefulness to quantitatively analyze high affinity protein ligand interactions employing a kinetic titration series for characterizing the interactions between two pairs of interaction patterns, in particular immunoglobulin G and protein G B1 as well as scFv IC16 and amyloid beta (1-42). Kinetic titration series are commonly used in surface plasmon resonance and involve sequential injections of analyte over a desired concentration range on a single ligand coated sensor chip without waiting for complete dissociation between the injections. We show that applying this method to biolayer interferometry is straightforward and i) circumvents problems in data evaluation caused by unavoidable sensor differences, ii) saves resources and iii) increases throughput if screening a multitude of different analyte/ligand combinations.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>25229647</pmid><doi>10.1371/journal.pone.0106882</doi><oa>free_for_read</oa></addata></record> |
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subjects | Biochemistry Biology and Life Sciences Biosensors Data analysis Design Dissociation Experiments Exports Immunoglobulin G Immunoglobulins Interferometry Interferometry - methods Kinetics Ligands Medicine and Health Sciences Physical Sciences Protein Binding Protein G Protein interaction Proteins Sensors Surface Plasmon Resonance Titration |
title | Kinetic titration series with biolayer interferometry |
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