The solubility of fibrinogen in solutions containing dextrans of various molecular weights (<i>Short Communication</i>)

Rampling, M.W.

doi:10.1042/bj1430767

Cited by 12 publications

(2 citation statements)

References 11 publications

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“…These two concentrations are relevant for understanding the behavior of surfaces in physiological conditions since molar concentrations of 7 μM are in the normal range for Fib in plasma, while a 0.30 mM concentration is close to that of albumin in serum 39 . Fib could not be studied at the higher concentration because it falls beyond its solubility limit 40 .…”

Section: Resultsmentioning

confidence: 99%

Modulation of Protein Fouling and Interfacial Properties at Carbon Surfaces via Immobilization of Glycans Using Aryldiazonium Chemistry

Zen

Angione

Behan

et al. 2016

Sci Rep

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Carbon materials and nanomaterials are of great interest for biological applications such as implantable devices and nanoparticle vectors, however, to realize their potential it is critical to control formation and composition of the protein corona in biological media. In this work, protein adsorption studies were carried out at carbon surfaces functionalized with aryldiazonium layers bearing mono- and di-saccharide glycosides. Surface IR reflectance absorption spectroscopy and quartz crystal microbalance were used to study adsorption of albumin, lysozyme and fibrinogen. Protein adsorption was found to decrease by 30–90% with respect to bare carbon surfaces; notably, enhanced rejection was observed in the case of the tested di-saccharide vs. simple mono-saccharides for near-physiological protein concentration values. ζ-potential measurements revealed that aryldiazonium chemistry results in the immobilization of phenylglycosides without a change in surface charge density, which is known to be important for protein adsorption. Multisolvent contact angle measurements were used to calculate surface free energy and acid-base polar components of bare and modified surfaces based on the van Oss-Chaudhury-Good model: results indicate that protein resistance in these phenylglycoside layers correlates positively with wetting behavior and Lewis basicity.

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Section: Resultsmentioning

confidence: 99%

Modulation of Protein Fouling and Interfacial Properties at Carbon Surfaces via Immobilization of Glycans Using Aryldiazonium Chemistry

Zen

Angione

Behan

et al. 2016

Sci Rep

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“…Because Dextran was known to precipitate fibrinogen in blood (Rampling, 1974), it could not be used as a viscous cosolvent, as had been done for A/S latex spheres covalently bearing monoclonal IgG and cross-linked by Protein G (Kwong et al, 1996). Instead, Ficoll 400 (Pharmacia Biotech) at a concentration of 19% w/v was found to be a suitable viscous cosolvent, with a suspending medium viscosity of 20 mPa/s at 23°C.…”

Section: Suspending Mediummentioning

confidence: 99%

Time and Force Dependence of the Rupture of Glycoprotein IIb-IIIa-Fibrinogen Bonds between Latex Spheres

Goldsmith

McIntosh

Shahin

et al. 2000

Biophysical Journal

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We studied the shear-induced breakup of doublets of aldehyde/sulfate (A/S) latex spheres covalently linked with purified platelet GPIIb-IIIa receptor, and cross-linked by fibrinogen. Flow cytometry with fluorescein isothiocyanate-fibrinogen showed than an average of 22,500 molecules of active GPIIb-IIIa were captured per sphere, with a mean K(d) = 56 nM for fibrinogen binding. The spheres, suspended in buffered 19% Ficoll 400 containing 120 or 240 pM fibrinogen, were subjected to Couette flow in a counter-rotating cone-plate rheoscope. Doublets, formed by two-body collisions at low shear rate (G = 8 s(-1)) for < or =15 min, were subjected to shear stress from 0.6 to 2.9 Nm(-2), their rotations recorded until they broke up or were lost to view. Although breakup was time dependent, occurring mostly in the first 2 rotations after the onset of shear, the percentage of doublets broken up after 10 rotations were almost independent of normal hydrodynamic force, F(n): at 240 pN, 15.6, 16.0, and 17.0% broke up in the force range 70-150 pN, 150-230 pN, and 230-310 pN. Unexpectedly, at both [fibrinogen], the initial rate of breakup was highest in the lowest force range, and computer simulation using a stochastic model of breakup was unable to simulate the time course of breakup. When pre-sheared at low G for >15 min, no doublets broke up within 10 rotations at 70 < F(n) < 310 pN; it required >3 min shear (>1110 rotations) at F(n) = 210 pN for significant breakup to occur. Other published work has shown that binding of fibrinogen to GPIIb-IIIa immobilized on plane surfaces exhibits an initial fast reversible process with relative low affinity succeeded by transformation of GPIIb-IIIa to a stable high-affinity complex. We postulate that most doublet breakups observed within 10 rotations were from a population of young doublets having low numbers of bonds, by dissociation of the initial receptor complex relatively unresponsive to force. The remaining, older doublets with GPIIb-IIIa in the high-affinity complex were not broken up in the time or range of forces studied.

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Interactions between dextran, fibrinogen and plasma membranes

Rampling

1976

Biochemical Pharmacology

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The solubility of fibrinogen in solutions containing dextrans of various molecular weights (Short Communication)

Cited by 12 publications

References 11 publications

Modulation of Protein Fouling and Interfacial Properties at Carbon Surfaces via Immobilization of Glycans Using Aryldiazonium Chemistry

Modulation of Protein Fouling and Interfacial Properties at Carbon Surfaces via Immobilization of Glycans Using Aryldiazonium Chemistry

Time and Force Dependence of the Rupture of Glycoprotein IIb-IIIa-Fibrinogen Bonds between Latex Spheres

Interactions between dextran, fibrinogen and plasma membranes

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