Blood plasma coagulation studied by surface plasmon resonance

Vikinge, Trine P.; Hansson, Kenny M.; Benesch, Johan; Johansen, Knut; Rånby, Mats; Lindahl, Tomas; Lundstroem, Ingemar; Tengvall, Pentti

doi:10.1117/12.336920

Cited by 10 publications

(14 citation statements)

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“…SPR has a small sensing depth, typically around 20-30% of the wavelength of the incident light beam (approximately 200 nm) making it a surface-or near-surface-sensitive method. Vikinge et al [47] report representative SPR response curves for experiments involving blood plasma and different thromboplastin concentrations, the SPR response change usually being interpreted as a change in refractive index at the sensor/liquid interface.…”

Section: Surface Plasmon Resonance and Quartz Crystal Microbalance-bamentioning

confidence: 98%

“…The SPR technique was more sensitive to cell-surface interactions than to fibrin formation in whole blood during coagulation, while the FOR technique was equally sensitive to coagulation in whole blood and plasma. It is noteworthy that despite its force measuring capability and its recent application in studies of the tensile properties of fluids [49], the atomic force microscope has rarely been exploited in coagulation studies [50] being mainly limited to imaging sensor surfaces involved in clotting experiments, in conjunction with SPR work [47].…”

Section: Surface Plasmon Resonance and Quartz Crystal Microbalance-bamentioning

confidence: 99%

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Rheometry and associated techniques for blood coagulation studies

Evans

Hawkins

Lawrence

et al. 2008

Medical Engineering & Physics

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Section: Surface Plasmon Resonance and Quartz Crystal Microbalance-bamentioning

confidence: 98%

Section: Surface Plasmon Resonance and Quartz Crystal Microbalance-bamentioning

confidence: 99%

Rheometry and associated techniques for blood coagulation studies

Evans

Hawkins

Lawrence

et al. 2008

Medical Engineering & Physics

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“…The binding of an analyte in the flow phase to a ligand immobilized on a sensor surface is measured in real time without the need of labeling (15). Although not all parameters of an extracorporeal flow system can be mimicked in a Biacore system, SPR has been used for a variety of purposes including the investigation of interactions between heparin and coagulation proteins (16,17) and has been employed in this study to analyze the binding kinetics of selected plasma proteins such as antithrombin III (AT3), thrombin, prothrombin, and fibrinogen to immobilized heparin in more detail.…”

mentioning

confidence: 99%

Plasma Protein Binding Properties to Immobilized Heparin and Heparin–Albumin Conjugate

et al. 2007

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Selective adhesion of plasma proteins to immobilized heparin is considered to be beneficial regarding hemocompatibility of foreign materials in contact with blood. Prothrombin, thrombin, antithrombin III (AT3), and fibrinogen were selected for analysis in an experimental model. Biomolecular interaction analysis employing surface plasmon resonance was utilized to record and analyze their binding properties in real time. Biotinylated heparin, heparin-albumin conjugate, and albumin, respectively, were immobilized onto streptavidin-coated sensors as ligands. Prothrombin did not bind to any of the ligand surfaces and no specific binding of any of the plasma proteins to albumin was observed. Binding kinetics of thrombin to heparin and to heparin-albumin conjugate were calculated using two different methods. For heparin, identical K(D)(equilibrium dissociation constant) values of 61 x 10(-9) M were obtained with both methods. For the conjugate, only slightly different K(D) values of 111 x 10(-9) and 104 x 10(-9) M, respectively, were calculated. The affinity of thrombin toward the heparin-coated surface proved to be higher than its affinity toward the heparin conjugate. The binding pattern of AT3 to both heparin and heparin-albumin conjugate, although specific, was biphasic, possibly due to a conformational change during the binding process. Steady-state kinetic analysis revealed a K(D) value of 281 +/- 24 x 10(-9) M for the heparin surface. For the conjugate surface, a K(D) of 53 +/- 5 x 10(-9) M was calculated, indicating a higher affinity toward heparin-albumin conjugate. A high-affinity binding of fibrinogen to high-density surfaces of both heparin and the conjugate was observed. However, as binding to low-density surfaces was considerably reduced, specificity remained uncertain.

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“…For convenience, these articles are subdivided into general biological categories: proteins, antibodies, cell surface receptors, 283-337 peptides, small molecules, oligonucleotides, lipids and self-assembled monolayers, extracellular matrix, carbohydrates, [533][534][535][536][537][538][539][540][541][542] particles and viruses, [543][544][545] crude analytes, [546][547][548] and other configurations. [549][550][551][552][553][554] Forty-nine articles describe work performed using other optical biosensor instrumentation. Thirty-one describe studies using the IAsys evanscent wave technology (Affinity Sensors, Franklin, MA; www.affinity-sensors.com); eight using SPR-670 (Nippon Laser and Electronics Laboratory, Hokkaido, Japan; www.nle-lab.co.jp/English/ ZO-HOME.htm); [586][587][588][589][590][591][592][593] four using IBIS (Windsor Scientific Limited, Berks, UK; www.ibis-spr.nl); [594][595][596][597] two using the instrument manufactured by Johnson & Johnson Orthoclinical Diagnostics, Ltd (Chalfont St Giles, UK; www.jnj.com); [598][599] two using Spreeta (Texas Instruments, Dallas, TX; www.ti.com/sc/docs/products/ msp/control/spreeta); 600, 601 and two using another platform.…”

Section: Reviews Theory and Methodologymentioning

confidence: 99%

Survey of the year 2000 commercial optical biosensor literature

Rich

Myszka

2001

J of Molecular Recognition

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We have compiled a comprehensive list of the articles published in the year 2000 that describe work employing commercial optical biosensors. Selected reviews of interest for the general biosensor user are highlighted. Emerging applications in areas of drug discovery, clinical support, food and environment monitoring, and cell membrane biology are emphasized. In addition, the experimental design and data processing steps necessary to achieve high-quality biosensor data are described and examples of well-performed kinetic analysis are provided.

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Blood plasma coagulation studied by surface plasmon resonance

Cited by 10 publications

References 0 publications

Rheometry and associated techniques for blood coagulation studies

Rheometry and associated techniques for blood coagulation studies

Plasma Protein Binding Properties to Immobilized Heparin and Heparin–Albumin Conjugate

Survey of the year 2000 commercial optical biosensor literature

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