Survey of the year 2003 commercial optical biosensor literature

Rich, Rebecca L.; Myszka, David G.

doi:10.1002/jmr.726

Cited by 197 publications

(48 citation statements)

References 921 publications

(159 reference statements)

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“…References 4, 10, 11, 13, and 18 describe the SPR phenomenon, compare and contrast the different platforms and sensor surfaces that are available, and outline how optical biosensors are implemented in studying a range of interactions. Our surveys of the 2003 and 2004 literature highlight recently published work that demonstrates the wealth of information available from well-designed and properly executed biosensor experiments [15,16].…”

Section: Reviews Methods and Theorymentioning

confidence: 99%

Survey of the year 2005 commercial optical biosensor literature

2006

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We identified 1113 articles (103 reviews, 1010 primary research articles) published in 2005 that describe experiments performed using commercially available optical biosensors. While this number of publications is impressive, we find that the quality of the biosensor work in these articles is often pretty poor. It is a little disappointing that there appears to be only a small set of researchers who know how to properly perform, analyze, and present biosensor data. To help focus the field, we spotlight work published by 10 research groups that exemplify the quality of data one should expect to see from a biosensor experiment. Also, in an effort to raise awareness of the common problems in the biosensor field, we provide side-by-side examples of good and bad data sets from the 2005 literature.

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Section: Reviews Methods and Theorymentioning

confidence: 99%

Survey of the year 2005 commercial optical biosensor literature

2006

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“…All experiments were conducted in 1% methanol, 10% glycerol, 100 mM potassium phosphate (pH 7.4), at flow rate of 100 μl/min, and at 10 °C unless stated otherwise. SPR data were double referenced [31][32][33] and analyzed with Biaevaluation software 4.1 (Biacore AB). Sensorgrams were corrected for organic co-solvent effects [35], but as witnessed by others the use of methanol as the organic co-solvent and the use of suitable control surfaces made correction factors negligible [36].…”

Section: Surface Plasmon Resonancementioning

confidence: 99%

“…All experiments were conducted in 1% methanol, 10% glycerol, 100 mM potassium phosphate (pH 7.4), at flow rate of 100 μl/min, and at 10 °C unless stated otherwise. SPR data were double referenced [31][32][33] During curve fitting and modeling, it was observed that the 'analyte heterogeneity' model contained within the BIAevaluation software consistently fit best to the data, even though experiments were run with chromatographically pure, chirally-resolved, diastereomers of either ITZ or KTZ. This initially surprising result is easily understood upon comparison of the differential equations describing heteroanalyte binding and those describing parallel trajectories for a single analyte.…”

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confidence: 99%

Surface Plasmon Resonance Analysis of Antifungal Azoles Binding to CYP3A4 with Kinetic Resolution of Multiple Binding Orientations

et al. 2006

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The heme-containing Cytochrome P450s (CYPs) are a major enzymatic determinant of drug clearance and drug-drug interactions. The CYP3A4 isoform is inhibited by antifungal imidazoles or triazoles, which form low spin heme iron complexes via formation of a nitrogen-ferric iron coordinate bond. However, CYP3A4 also slowly oxidizes the antifungal itraconazole (ITZ) at a site that is ∼ 25 Å from the triazole nitrogens, suggesting that large antifungal azoles can adopt multiple orientations within the CYP3A4 active site. Here, we report a surface plasmon resonance (SPR) analysis with kinetic resolution of two binding modes of ITZ, and the related drug ketoconazole (KTZ). SPR reveals a very slow off-rate for one binding orientation. Multiphasic binding kinetics are observed and one of the two binding components resolved by curve-fitting exhibits 'equilibrium overshoot'. Pre-loading of CYP3A4 with the heme ligand imidazole abolishes this component of the antifungal azole binding trajectories, and it eliminates the conspicuously slow off-rate. The fractional populations of CYP3A4 complexes corresponding to different drug orientations can be manipulated by altering the duration of the pulse of drug exposure. UV-vis difference absorbance titrations yield low spin spectra and K D values that are consistent with the high affinity complex resolved by SPR. These results demonstrate that ITZ and KTZ bind in multiple orientations, including a catalytically productive mode and a slowly-dissociating inhibitory mode. Most importantly, they provide the first example of an SPR-based method for the kinetic characterization of drug binding to any human CYP, including mechanistic insight not available from other methods. Keywords protein-ligand interactions; tight binding inhibitors; drug metabolism; drug interactionsThe hepatic and intestinal heme-containing Cytochrome P450s (CYPs) 1 oxidize most drugs, and thus play a critical role in their metabolism and disposition [1][2][3]. Among the various human CYP isoforms, CYP3A4 contributes most to drug metabolism. CYP3A4 exhibits complex allosteric kinetics, which may result from drug-drug interactions on a single CYP molecule through multiple drug binding, as suggested by steady state kinetic behavior [4][5][6], large active sites observed in crystal structures [7][8][9][10] and spectroscopic studies [11]. Complex kinetics † This work was supported by NIH grants GM32165 (WMA, NI, KLK) and GM07750 (JTP). * Corresponding author: Tel: (206) FAX: (206) [12][13][14][15], and equilibrium optical titrations that rely on the inhibitor-or substrate-dependent changes in ferric spin state equilibrium [16][17][18]. The complexity of CYP kinetics severely impedes prediction of drug clearance and drug-drug interactions [12][13][14][15]19]. Clearly, new methods are required to elucidate the molecular basis of CYP allosterism and complex inhibitor or substrate binding.The antifungal azoles, including ketoconazole (KTZ) and itraconazole (ITZ), historically have been considered to be potent inh...

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“…In some cases, non specific adsorption can be reduced by adding CM dextran sodium salt in the samples (Karlsson et al, 1993;Yang et al, 2005). To date, BIAcore and CM5 chip are most widely used equipment and sensor chip (Rich and Myszka, 2005;Rich and Myszka, 2007).…”

Section: Introductionmentioning

confidence: 99%

A simple method for quantification of interferon-2b through surface plasmon resonance technique

Ramanan¹,

Ling²,

Tey³

et al. 2010

Afr. J. Biotechnol.

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A rapid and efficient immunoassay method for quantification of interferon-α2b using surface plasmon resonance was developed with BIAcore 3000 as a sensor. Two different levels of anti-interferon monoclonal antibody were immobilized onto a CM5 chip using an amine coupling method. Similar binding ratio was observed for both the ligand densities. There was no steric hindrance and loss of antibody activity even at higher ligand density (> 22,000 RU). The sensitivity of the assay was increased up to 45% with the increment in ligand density from 15,400 to 22,360 RU. The binding between interferon-α2b and anti-interferon monoclonal antibody was predominantly controlled by mass transfer rate and the relationship was found linear, ranged from 5 to 400 ng/mL. Total cycle time per analysis was less than 8 min and required only 5 µL of sample injection.

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Survey of the year 2003 commercial optical biosensor literature

Cited by 197 publications

References 921 publications

Survey of the year 2005 commercial optical biosensor literature

Survey of the year 2005 commercial optical biosensor literature

Surface Plasmon Resonance Analysis of Antifungal Azoles Binding to CYP3A4 with Kinetic Resolution of Multiple Binding Orientations

A simple method for quantification of interferon-2b through surface plasmon resonance technique

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