Comparative analyses of a small molecule/enzyme interaction by multiple users of Biacore technology

Cannon, Michelle J.; Papalia, Giuseppe A.; Navrátilová, Iva; Fisher, Robert J.; Roberts, Lindsey R.; Worthy, Karen M.; Stephen, Andrew; Marchesini, Gerardo; Collins, Edward J.; Casper, D.; Qiu, Huawei; Satpaev, Daulet K.; Liparoto, Stefano F.; Rice, Dax A.; Gorshkova, Inna; Darling, Ryan J.; Bennett, D. R.; Sekar, M.S.; Hommema, Eric; Liang, Amy; Day, Eric S.; Inman, Jean; Karlicek, Shannon; Ullrich, Stephen J.; Hodges, Dianne; Chu, Teresa; Sullivan, Eric; Simpson, Jane; Rafique, Ashique; Luginbühl, Béatrice; Westin, Susanne Nyholm; Bynum, M; Cachia, Paul J.; Li, Yue Jin; Kao, Daniel J.; Neurauter, Amy; Wong, Melanie; Swanson, Michael; Myszka, David G.

doi:10.1016/j.ab.2004.02.027

Cited by 73 publications

(58 citation statements)

References 11 publications

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“…The fitting model also contained a floating term to correct for slight changes in the bulk refractive index of analyte solutions. SPR data were double-referenced [35], i.e. corrected for analyte solution responses as well as pure buffer responses, the former reflecting bulk refractive index changes and the latter any background instrumental "noise".…”

Section: Surface Plasmon Resonance Analysesmentioning

confidence: 99%

Lipid transfer protein binding of unmodified natural lipids as assessed by surface plasmon resonance methodology

Kernstock

Girotti

2007

Analytical Biochemistry

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A new approach for analyzing lipid-lipid transfer protein interactions is described. The transfer protein is genetically engineered for expression with a C-terminal biotinylated peptide extension (AviTag ® ). This allows protein anchoring to a streptavidin-coated chip for surface plasmon resonance (SPR)-based assessment of lipid binding. Sterol carrier protein-2 (SCP-2), involved in the intracellular trafficking of cholesterol, fatty acids and other lipids, was selected as the prototype. Biotinylated SCP-2 (bSCP-2) was expressed in E. coli, purified to homogeneity by mutated streptavidin (SoftLink ® ) affinity chromatography, and confirmed by mass spectrometry to contain one biotin group at the expected position. Intermembrane [ 14 C]cholesterol transfer was strongly enhanced by bSCP-2, demonstrating that it was functional. Using bSCP-2 immobilized on a Biacore streptavidin chip, we determined on-and off-rate constants along with equilibrium dissociation constants for the following analytes: oleic acid, linoleic acid, cholesterol, and fluorophore (NBD)-derivatized cholesterol. The dissociation constant for NBD-cholesterol was similar to that determined by fluorescence titration for SCP-2 in solution, thus validating the SPR approach. This method can be readily adapted to other transfer proteins and has several advantages over existing techniques for measuring lipid binding, including (i) ability to study lipids in their natural states, i.e. without relatively large reporter groups; and (ii) ability to measure on-and off-rate constants as well as equilibrium constants.

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Section: Surface Plasmon Resonance Analysesmentioning

confidence: 99%

Lipid transfer protein binding of unmodified natural lipids as assessed by surface plasmon resonance methodology

Kernstock

Girotti

2007

Analytical Biochemistry

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“…We also created a reference surface by performing the aminecoupling procedure in the absence of CA II on another flow cell surface. We dissolved acetazolamide (ACZ; Sigma) in Dulbecco's phosphate-buffered saline (Sigma), and sequentially injected this solution over each surface at 100 l/min for 1 min, followed by a 7-min dissociation interval, similar to previous investigators (26). The pure SLC4-Ct peptides, diluted in HBS-EP buffer (10 mM HEPES, pH 7.4, 150 mM NaCl, 3 mM EDTA, 0.005% surfactant P20; Biacore AB) containing 100 M tris(2-carboxyethyl)phosphine hydrochloride (Sigma), were injected over the CA II and reference surfaces at 25 l/min for 2.4 min followed by a 5-min dissociation interval.…”

Section: Solid-phase Binding Assays With Spr Detectionmentioning

confidence: 99%

“…We then subtracted the mean response of 2-3 buffer injections from each active-surface sensorgram to correct for drift in the data. To fit kinetic parameters to the ACZ binding data, we used a 1:1 Langmuir binding model that includes a correction for mass transfer effects (26).…”

Section: Data Analysis and Statisticsmentioning

confidence: 99%

Evidence against a Direct Interaction between Intracellular Carbonic Anhydrase II and Pure C-terminal Domains of SLC4 Bicarbonate Transporters

Piermarini

Kim

Boron

2007

Journal of Biological Chemistry

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Based on solid-phase binding assays with enzyme-linked immunosorbent assay detection, previous investigators suggested that intracellular carbonic anhydrase II (CA II) interacts at high affinity with the C-terminal (Ct) domains of SLC4 bicarbonate-transport proteins, expressed as glutathione S-transferase (GST) fusion proteins, to form functional HCO 3 ؊ metabolons. Here we re-evaluated this protein-protein interaction using two solid-phase binding assays. We first compared the ability of the Ct domain of three SLC4 transporters, SLC4-A1 (AE1), SLC4-A4 (NBCe1), and SLC4-A8 (NDCBE), to bind immobilized CA II, using enzyme-linked immunosorbent assay detection. We found that when expressed as GST fusion proteins, all three bind to CA II (K d 300 -600 nM) better than does pure GST. However, we detected no binding of pure SLC4-Ct peptides to immobilized CA II. Second, we reversed assay orientation by immobilizing the SLC4-Ct fusion proteins or peptides. We found that more CA II binds to GST than to any of the three GST-SLC4-Ct fusion proteins. Furthermore, we detected no binding of CA II to any of the immobilized pure SLC4-Ct peptides. Finally, we used surface plasmon resonance to detect possible rapid interactions between CA II and the pure peptides. Although we detected acetazolamide binding to immobilized CA II and specific antibodies binding to immobilized SLC4-Ct peptides, we detected no binding of CA II to immobilized SLC4-Ct or vice versa. Thus, although an HCO 3 metabolon may exist, CA II cannot bind directly to pure SLC4-Ct peptides and can bind to GST-SLC4-Ct fusion proteins only when the CA II is immobilized and the fusion protein is soluble, and not vice versa.

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“…Of the 678 articles that stated which Biacore platform was used, most utilized 2000 and 3000 platforms [222, (33%) and 249 (37%), respectively]. Investigators also reported data obtained from Biacore X (129, 19%) and 1000 (57, 8%), as well as from S51 [273,818,831,843,865], J [223,285,737,745,759], Q [892,905,907,910,913], Bialite [492,726,787,873] and Probe [348] platforms.…”

Section: Instrumentsmentioning

confidence: 94%

Survey of the year 2004 commercial optical biosensor literature

Rich

Myszka

2005

J of Molecular Recognition

115

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The year 2004 represents a milestone for the biosensor research community: in this year, over 1000 articles were published describing experiments performed using commercially available systems. The 1038 papers we found represent a $ 10% increase over the past year and demonstrate that the implementation of biosensors continues to expand at a healthy pace. We evaluated the data presented in each paper and compiled a 'top 10' list. These 10 articles, which we recommend every biosensor user reads, describe wellperformed kinetic, equilibrium and qualitative/screening studies, provide comparisons between binding parameters obtained from different biosensor users, as well as from biosensor-and solution-based interaction analyses, and summarize the cutting-edge applications of the technology. We also re-iterate some of the experimental pitfalls that lead to sub-optimal data and over-interpreted results. We are hopeful that the biosensor community, by applying the hints we outline, will obtain data on a par with that presented in the 10 spotlighted articles. This will ensure that the scientific community at large can be confident in the data we report from optical biosensors.

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Comparative analyses of a small molecule/enzyme interaction by multiple users of Biacore technology

Cited by 73 publications

References 11 publications

Lipid transfer protein binding of unmodified natural lipids as assessed by surface plasmon resonance methodology

Lipid transfer protein binding of unmodified natural lipids as assessed by surface plasmon resonance methodology

Evidence against a Direct Interaction between Intracellular Carbonic Anhydrase II and Pure C-terminal Domains of SLC4 Bicarbonate Transporters

Survey of the year 2004 commercial optical biosensor literature

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