Optimization of surface plasmon resonance experiments: Case of high mobility group box 1 (HMGB1) interactions

© 2016 Elsevier Inc. All rights reserved. Surface plasmon resonance (SPR) is a powerful technique for evaluating protein-protein interactions in real time. However, inappropriately optimized experiments can often lead to problems in the interpretation of data, leading to unreliable kinetic constants...

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Main Authors: Anggayasti, W., Mancera, Ricardo, Bottomley, Steven, Helmerhorst, Erik
Format: Journal Article
Published: 2016
Online Access:http://hdl.handle.net/20.500.11937/42158
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author Anggayasti, W.
Mancera, Ricardo
Bottomley, Steven
Helmerhorst, Erik
author_facet Anggayasti, W.
Mancera, Ricardo
Bottomley, Steven
Helmerhorst, Erik
author_sort Anggayasti, W.
building Curtin Institutional Repository
collection Online Access
description © 2016 Elsevier Inc. All rights reserved. Surface plasmon resonance (SPR) is a powerful technique for evaluating protein-protein interactions in real time. However, inappropriately optimized experiments can often lead to problems in the interpretation of data, leading to unreliable kinetic constants and binding models. Optimization of SPR experiments involving "sticky" proteins, or proteins that tend to aggregate, represents a typical scenario where it is important to minimize errors in the data and the kinetic analysis of those data. This is the case of High Mobility Group Box 1 and the receptor of advanced glycation end products. A number of improvements in protein purification, buffer composition, immobilization conditions, and the choice of flow rate are shown to result in substantial improvements in the accurate characterization of the interactions of these proteins and the derivation of the corresponding kinetic constants.
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institution Curtin University Malaysia
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spelling curtin-20.500.11937-421582017-09-13T14:23:34Z Optimization of surface plasmon resonance experiments: Case of high mobility group box 1 (HMGB1) interactions Anggayasti, W. Mancera, Ricardo Bottomley, Steven Helmerhorst, Erik © 2016 Elsevier Inc. All rights reserved. Surface plasmon resonance (SPR) is a powerful technique for evaluating protein-protein interactions in real time. However, inappropriately optimized experiments can often lead to problems in the interpretation of data, leading to unreliable kinetic constants and binding models. Optimization of SPR experiments involving "sticky" proteins, or proteins that tend to aggregate, represents a typical scenario where it is important to minimize errors in the data and the kinetic analysis of those data. This is the case of High Mobility Group Box 1 and the receptor of advanced glycation end products. A number of improvements in protein purification, buffer composition, immobilization conditions, and the choice of flow rate are shown to result in substantial improvements in the accurate characterization of the interactions of these proteins and the derivation of the corresponding kinetic constants. 2016 Journal Article http://hdl.handle.net/20.500.11937/42158 10.1016/j.ab.2015.12.024 restricted
spellingShingle Anggayasti, W.
Mancera, Ricardo
Bottomley, Steven
Helmerhorst, Erik
Optimization of surface plasmon resonance experiments: Case of high mobility group box 1 (HMGB1) interactions
title Optimization of surface plasmon resonance experiments: Case of high mobility group box 1 (HMGB1) interactions
title_full Optimization of surface plasmon resonance experiments: Case of high mobility group box 1 (HMGB1) interactions
title_fullStr Optimization of surface plasmon resonance experiments: Case of high mobility group box 1 (HMGB1) interactions
title_full_unstemmed Optimization of surface plasmon resonance experiments: Case of high mobility group box 1 (HMGB1) interactions
title_short Optimization of surface plasmon resonance experiments: Case of high mobility group box 1 (HMGB1) interactions
title_sort optimization of surface plasmon resonance experiments: case of high mobility group box 1 (hmgb1) interactions
url http://hdl.handle.net/20.500.11937/42158