Rapid paper diagnostic for plasma fibrinogen concentration

Bialkower, Marek; McLiesh, Heather; Manderson, Clare A.; Tabor, Rico F.

doi:10.1039/c9an00616h

Cited by 15 publications

(16 citation statements)

References 62 publications

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“…Similar melting temperatures were obtained for fibrinogen alone or in the presence of resveratrol ( Figure 3 A,B), suggesting that resveratrol does not significantly ( p > 0.05) affect fibrinogen folding and stability. The melting temperature was 53.2 ± 0.6 °C for fibrinogen alone and 53.9 ± 0.48 °C for fibrinogen in the presence of resveratrol, which was similar to previously published results [ 8 ]. This melting temperature corresponds to the melting of the terminal D regions of fibrinogen [ 26 ].…”

Section: Resultssupporting

confidence: 91%

“…Plasma consists of over 100 proteins, the major ones being albumin, α-globulins, β-globulins, γ-globulins and fibrinogen. Fibrinogen is a 340 kDa glycoprotein composed of three pairs of chains with an (AαBβγ)2 structure [ 7 ] that circulates in the bloodstream at concentrations of 2 to 4 mg/mL (5.9–11.8 μM) [ 8 ]. Fibrinogen functions in the process of hemostasis, whereby during blood vessel injury the aggregation of platelets occurs through the interaction of fibrinogen with IIb/IIIa integrin on the surface of platelets, linking adjacent platelets and coagulating the blood (primary hemostasis) [ 9 ].…”

Section: Introductionmentioning

confidence: 99%

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Fibrinogen Increases Resveratrol Solubility and Prevents it from Oxidation

Gligorijević

Radomirović

Rajković

et al. 2020

Foods

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The French paradox describes a lower incidence of cardiovascular problems despite a high intake of saturated fats. This phenomenon was associated with higher consumption of red wine, as it was later discovered that the presence of antioxidants, including resveratrol, have beneficial effects. We hypothesized that resveratrol may have a more direct role in protection from harmful oxidation, presumably through binding to important proteins of the blood coagulation process. Spectrofluorimetry demonstrated that resveratrol is capable of binding to fibrinogen, the main protein in the coagulation process, which is also important as a food additive. Various spectroscopic methods determined that binding does not cause fibrinogen unfolding or destabilization since protein melting temperature remains unchanged. A mutually protective effect against the free radical-induced oxidation of polyphenol and fibrinogen was found. The presence of fibrinogen caused only a negligible masking effect of the antioxidative abilities of resveratrol, measured by a reduction of hexacyanoferrate (III), while greatly increasing its solubility in an aqueous environment, thus increasing its potential bioavailability. Due to its interaction with fibrinogen, resveratrol may serve as an antioxidant at the site of injury. The antioxidative effect of resveratrol may also protect and thus keep the desired characteristics of fibrinogen during the application of this protein as a food additive.

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Section: Resultssupporting

confidence: 91%

Section: Introductionmentioning

confidence: 99%

Fibrinogen Increases Resveratrol Solubility and Prevents it from Oxidation

Gligorijević

Radomirović

Rajković

et al. 2020

Foods

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“…Fibrinogen, a primary component of human plasma protein, plays a vital role in the process of blood coagulation [ 1 ] and usually circulates at a concentration of between 2 and 4 g/L in the human body [ 2 ]. Fibrinogen treatments for patients with massive bleeding are essential for survival [ 3 ], and the amount of fibrinogen administered to trauma patients is positively correlated with reductions in mortality [ 4 ].…”

Section: Introductionmentioning

confidence: 99%

Engineered polymer nanoparticles incorporating l-amino acid groups as affinity reagents for fibrinogen

Zhu

Liu

et al. 2021

Journal of Pharmaceutical Analysis

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Synthetic polymer hydrogel nanoparticles (NPs) were developed to function as abiotic affinity reagents for fibrinogen. These NPs were made using both temperature-sensitive N-isopropyl acrylamide (NIPAm) and l -amino acid monomers. Five kinds of l -amino acids were acryloylated to obtain functional monomers: l -phenylalanine (Phe) and l -leucine (Leu) with hydrophobic side chains, l -glutamic acid (Glu) with negative charges, and l -lysine (Lys) and l -arginine (Arg) with positive charges. After incubating the NPs with fibrinogen, γ-globulin, and human serum albumin (HSA) respectively, the NPs that incorporated N-acryloyl-Arg monomers (AArg@NPs) showed the strongest and most specific binding affinity to fibrinogen, when compared with γ-globulin and HSA. Additionally, the fibrinogen-AArg binding model had the best docking scores, and this may be due to the interaction of positively charged AArg@NPs and the negatively charged fibrinogen D domain and the hydrophobic interaction between them. The specific adsorption of AArg@NPs to fibrinogen was also confirmed by the immunoprecipitation assay, as the AArg@NPs selectively trapped the fibrinogen from a human plasma protein mixture. AArg@NPs had a strong selectivity for, and specificity to, fibrinogen and may be developed as a potential human fibrinogen-specific affinity reagent.

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“…An initial approach employed a vertically suspended paper substrate, with fibrinogen levels determined from the distance travelled by the sample up the strip. 15 However, the orientation of the device and the need for a fluid reservoir make it impractical for point-of-care use. Another approach utilized the permeability of the paper to fibrinogen.…”

mentioning

confidence: 99%

“…Paper-based devices have recently been applied to fibrinogen measurement. An initial approach employed a vertically suspended paper substrate, with fibrinogen levels determined from the distance travelled by the sample up the strip . However, the orientation of the device and the need for a fluid reservoir make it impractical for point-of-care use.…”

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confidence: 99%

Paper-Based Lateral Flow Device for the Sustainable Measurement of Human Plasma Fibrinogen in Low-Resource Settings

et al. 2021

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Fibrinogen concentration is a major determinant of both clotting and bleeding risk. Clotting and bleeding disorders cause extensive morbidity and mortality, particularly in resource-poor and emergency settings. This is exacerbated by a lack of timely intervention informed by measurement of fibrinogen levels under conditions such as thrombosis or postpartum haemorrhage. There is an absence of simple, rapid, low-cost, and sustainable diagnostic devices for fibrinogen measurement that can be deployed in such environments. Paper-based analytical devices are of significant interest due to their potential for low-cost production, ease of use, and environmental sustainability. In this work, a device for measuring blood plasma fibrinogen using chromatography paper was developed. Wax printing was used to create hydrophobic structures to define the test channel and sample application zone. Test strips were modified with bovine thrombin. Plasma samples (22 μL) were applied, and the flow rate was monitored over 5 min. As the sample traversed the strip, clotting was induced by the conversion of soluble fibrinogen to insoluble fibrin. The flow rate and distance travelled by the sample were dependent on fibrinogen concentration. The device was able to measure fibrinogen concentration in the range of 0.5–7.0 ± 0.3 mg/mL ( p < 0.05, n = 24) and had excellent correlation with laboratory coagulometry in artificial samples ( r 2 = 0.9582, n = 60). Devices were also stable at 4–6 °C for up to 3 weeks.

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Rapid paper diagnostic for plasma fibrinogen concentration

Abstract: Fibrinogen is one of the first proteins to be depleted in heavily bleeding patients. In this study, we have developed a new paper-based diagnostic to quantify the fibrinogen concentration in blood at room temperature.

Cited by 15 publications

References 62 publications

Fibrinogen Increases Resveratrol Solubility and Prevents it from Oxidation

Fibrinogen Increases Resveratrol Solubility and Prevents it from Oxidation

Engineered polymer nanoparticles incorporating l-amino acid groups as affinity reagents for fibrinogen

Paper-Based Lateral Flow Device for the Sustainable Measurement of Human Plasma Fibrinogen in Low-Resource Settings

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