Surface plasmon resonance measurement of pH-induced responses of immobilized biomolecules: conformational change or electrostatic interaction effects?
Abstract: Recently, the observation of pH-induced conformational changes of biomolecules supported on carboxymethyldextran (CMD)-coated surfaces measured using surface plasmon resonance (SPR) has been reported. However, it is apparent that the evidence reported in the literature is ambiguous. The research presented in this paper describes investigations to study the changing SPR signal of immobilized biomolecules as a function of varying pH, to provide a detailed understanding of the origin of the pH-induced changes in the SPR profile. SPR measurements were performed with cytochrome c, concanavalin A, and poly-L-lysine, biomolecules that exhibit diverse conformational responses to changing pH, covalently immobilized onto CMD-coated supports. These SPR measurements were supported by circular dichroism (CD) solution studies. The SPR profiles recorded were not consistent with the conformational transitions of the biomolecules as observed using CD. An alternative explanation for the observed shifts in SPR is proposed, which explains the SPR profiles in terms of electrostatic interaction effects between the immobilized biomolecules and the carboxymethyldextran matrix.
Publication Date: 2002-10-17 PubMed ID: 12381366DOI: 10.1016/s0003-2697(02)00255-5Google Scholar: Lookup
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- Comparative Study
- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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This research investigates the effect of varying pH levels on the surface plasmon resonance (SPR) signals of immobilized biomolecules, aiming to understand whether the changes observed are due to conformational changes in the biomolecules or electrostatic interaction effects with the supporting material.
Overview of the Study
- This research aims to investigate the ambiguity that exists in the current literature regarding the pH-induced conformational changes of biomolecules supported on carboxymethyldextran (CMD)-coated surfaces.
- Surface plasmon resonance (SPR) is used as a method of recording the effects of changes in pH on immobilized biomolecules such as cytochrome c, concanavalin A, and poly-L-lysine.
- The study seeks to explain the varying SPR signals of these biomolecules, which exhibit diverse conformational responses to a change in pH.
Methodology
- These biomolecules are covalently immobilized onto CMD-coated surfaces, then subject to varying levels of pH.
- The SPR measurements taken are then supported by circular dichroism (CD) solution studies, which detect the altered conformations of the molecules in the solution.
Findings
- Interestingly, the recorded SPR profiles did not match the conformational changes observed in the biomolecules using the CD method. This observed discrepancy prompted the researchers to seek an alternative explanation.
Conclusion
- The researchers propose a different explanation for the observed shifts in SPR. They theorize that the changes in the SPR profiles could be due to the electrostatic interaction effects between the immobilized biomolecules and the CMD substrate, rather than being a direct result of the pH-induced conformational change of the biomolecules.
- This understanding forms the basis for further research and highlights the interplay of multiple factors that can influence SPR measurements of biomolecular structures.
Cite This Article
APA
Paynter S, Russell DA.
(2002).
Surface plasmon resonance measurement of pH-induced responses of immobilized biomolecules: conformational change or electrostatic interaction effects?
Anal Biochem, 309(1), 85-95.
https://doi.org/10.1016/s0003-2697(02)00255-5 Publication
Researcher Affiliations
- School of Chemical Sciences, University of East Anglia, Norwich, Norfolk NR4 7TJ, UK.
MeSH Terms
- Animals
- Canavalia / chemistry
- Circular Dichroism
- Concanavalin A / chemistry
- Concanavalin A / classification
- Cytochrome c Group / chemistry
- Dextrans / chemistry
- Horses
- Hydrogen-Ion Concentration
- Myocardium / chemistry
- Peptides
- Polylysine / chemistry
- Protein Conformation
- Protein Folding
- Reference Standards
- Static Electricity
- Surface Plasmon Resonance / methods
Citations
This article has been cited 8 times.- David S, Gheorghiu M, Daakour S, Munteanu RE, Polonschii C, Gáspár S, Barboiu M, Gheorghiu E. Real Time SPR Assessment of the Structural Changes of Adaptive Dynamic Constitutional Frameworks as a New Route for Sensing.. Materials (Basel) 2022 Jan 9;15(2).
- Steinegger A, Wolfbeis OS, Borisov SM. Optical Sensing and Imaging of pH Values: Spectroscopies, Materials, and Applications.. Chem Rev 2020 Nov 25;120(22):12357-12489.
- Vagrys D, Davidson J, Chen I, Hubbard RE, Davis B. Exploring IDP-Ligand Interactions: tau K18 as A Test Case.. Int J Mol Sci 2020 Jul 24;21(15).
- Lea WA, O'Neil PT, Machen AJ, Naik S, Chaudhri T, McGinn-Straub W, Tischer A, Auton MT, Burns JR, Baldwin MR, Khar KR, Karanicolas J, Fisher MT. Chaperonin-Based Biolayer Interferometry To Assess the Kinetic Stability of Metastable, Aggregation-Prone Proteins.. Biochemistry 2016 Sep 6;55(35):4885-908.
- Chumphukam O, Le TT, Cass AE. High efficiency acetylcholinesterase immobilization on DNA aptamer modified surfaces.. Molecules 2014 Apr 21;19(4):4986-96.
- Ghosh N, Gupta G, Boopathi M, Pal V, Singh AK, Gopalan N, Goel AK. Surface Plasmon Resonance Biosensor for Detection of Bacillus anthracis, the Causative Agent of Anthrax from Soil Samples Targeting Protective Antigen.. Indian J Microbiol 2013 Mar;53(1):48-55.
- Naik S, Brock S, Akkaladevi N, Tally J, McGinn-Straub W, Zhang N, Gao P, Gogol EP, Pentelute BL, Collier RJ, Fisher MT. Monitoring the kinetics of the pH-driven transition of the anthrax toxin prepore to the pore by biolayer interferometry and surface plasmon resonance.. Biochemistry 2013 Sep 17;52(37):6335-47.
- Hall WP, Modica J, Anker J, Lin Y, Mrksich M, Van Duyne RP. A conformation- and ion-sensitive plasmonic biosensor.. Nano Lett 2011 Mar 9;11(3):1098-105.
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