Models for electrostatic interactions between protein molecules and surfaces involved in blood clot formation

1974 ◽  
Vol 20 (1-2) ◽  
pp. 85-103 ◽  
Author(s):  
Barbara Abraham-Shrauner
Keyword(s):  
Electrostatic Interactions ◽  
Blood Clot ◽  
Clot Formation ◽  
Protein Molecules

The Haemocompatibility of Biomaterials In Vitro: Investigations on the Mechanism of the Whole-blood Clot Formation Test

1992 ◽  
Vol 20 (3) ◽  
pp. 390-395 ◽  
Author(s):  
Thomas Groth ◽  
Katrin Derdau ◽  
Frank Strietzel ◽  
Frank Foerster ◽  
Hartmut Wolf
Keyword(s):  
Whole Blood ◽  
Blood Clotting ◽  
Blood Clot ◽  
Formation Rate ◽  
Clot Formation ◽  
Coagulation Cascade ◽  
Contact Activation ◽  
Human Fibrinogen ◽  
Static Conditions

Twenty years ago Imai & Nose introduced a whole-blood clotting test for the estimation of haemocompatibility of biomaterials in vitro In our paper a modification of this assay is described and the mechanism of clot formation further elucidated. It was found that neither the inhibition of platelet function nor the removal of platelets from blood significantly changed the clot formation rate on glass and polyvinyl chloride in comparison to the rate tor whole blood. Scanning electron microscopy demonstrated that platelets were not involved in clot formation near the blood/biomaterial interface. Thus, it was concluded that the system of contact activation of the coagulation cascade dominates during clot formation under static conditions. The latter conclusion was supported by the fact that preadsorption of human serum albumin or human fibrinogen onto the glass plates used, decreased the clot formation rate in the same manner.

scholarly journals Anticoagulant Polyethylene Terephthalate Surface by Plasma-Mediated Fucoidan Immobilization

Polymers ◽  
2019 ◽  
Vol 11 (5) ◽  
pp. 750 ◽  
Author(s):  
Kadir Ozaltin ◽  
Marian Lehocky ◽  
Petr Humpolicek ◽  
Jana Pelkova ◽  
Antonio Di Martino ◽  
...  
Keyword(s):  
Polyethylene Terephthalate ◽  
Photoelectron Spectroscopy ◽  
Anticoagulant Activity ◽  
Blood Clot ◽  
Clot Formation ◽  
Thrombin Time ◽  
Air Plasma ◽  
Water Contact ◽  
Polymeric Biomaterials ◽  
Performance Surface

Biomaterial-based blood clot formation is one of the biggest drawbacks of blood-contacting devices. To avoid blood clot formation, their surface must be tailored to increase hemocompatibility. Most synthetic polymeric biomaterials are inert and lack bonding sites for chemical agents to bond or tailor to the surface. In this study, polyethylene terephthalate was subjected to direct current air plasma treatment to enhance its surface energy and to bring oxidative functional binding sites. Marine-sourced anticoagulant sulphated polysaccharide fucoidan from Fucus vesiculosus was then immobilized onto the treated polyethylene terephthalate (PET) surface at different pH values to optimize chemical bonding behavior and therefore anticoagulant performance. Surface properties of samples were monitored using the water contact angle; chemical analyses were performed by FTIR and X-ray photoelectron spectroscopy (XPS) and their anticoagulant activity was tested by means of prothrombin time, activated partial thromboplastin time and thrombin time. On each of the fucoidan-immobilized surfaces, anticoagulation activity was performed by extending the thrombin time threshold and their pH 5 counterpart performed the best result compared to others.

Physicochemical properties of protein-smectite and protein-Al(OH)x-smectite complexes

Clay Minerals ◽  
1995 ◽  
Vol 30 (4) ◽  
pp. 325-336 ◽  
Author(s):  
A. Violante ◽  
A. de Cristofaro ◽  
M.A. Rao ◽  
L. Gianfreda
Keyword(s):  
Physicochemical Properties ◽  
Clay Minerals ◽  
Adsorption Isotherms ◽  
Electrostatic Interactions ◽  
Clay Fraction ◽  
Electrostatic Forces ◽  
Molecular Weights ◽  
Protein Molecules ◽  
Isoelectric Points ◽  
Heating Treatment

AbstractProteins (catalase, albumin, pepsin and lysozyme with different molecular weights and isoelectric points) were differently adsorbed at pH 7.0 on the clay fraction of three raw Na-saturated smectites (Crook and Uri montmorillonites and one hectorite). The adsorption isotherms of proteins on clay minerals showed typical Langmuir characteristics. Lysozyme was adsorbed under the effect of electrostatic interactions between the opposite charges of clay surfaces and protein molecules, whereas catalase and albumin were adsorbed under the effect of non-electrostatic forces. Pepsin was held in relatively high amounts only on the surfaces of hectorite. Proteins were intercalated in the interlayers spaces of smectites, usually undergoing extensive unfolding. Protein-smectite complexes showed different behaviour to heating treatment. Some complexes remained practically unchanged after heating at 200°C. Presence of ‘wrecks’ of interlayered materials was found after heating at 500°C for two hours. The amounts of proteins adsorbed on the external and interlamellar surfaces of clay minerals, partially coated with OH-Al species, were much lower than those fixed on the clean clays. Only lysozyme was intercalated in chlorite-like complexes.

Sol-Gel Preparation of HAp-Coated Silica Macrospheres from Water Glass and their Protein Adsorption

2012 ◽  
Vol 529-530 ◽  
pp. 637-640
Author(s):  
Jie Li ◽  
Yuki Shirosaki ◽  
Satoshi Hayakawa ◽  
Artemis Stamboulis ◽  
Akiyoshi Osaka
Keyword(s):  
Water Glass ◽  
Electrostatic Interactions ◽  
Coating Layer ◽  
Sol Gel ◽  
Adsorption Model ◽  
Silica Source ◽  
Layer Adsorption ◽  
Protein Molecules ◽  
Gel Preparation ◽  
Ca Alginate

Silica gel macrospheres of 2~4 mm in size, and wrapped with Ca-alginate chelate film were prepared as the substrate for hydroxyapatite coating layer, using water glass as the silica source. Those Ca-SiO2 macrospheres were soaked in a 1:1 (volume) mixture of ethanol and 0.1 M Na2HPO4 to deposit hydroxyapatite layer (HAp-SiO2 macrospheres). Adsorption of bovine serum albumin and egg lysozyme on those Ca-SiO2 and HAp-SiO2 macrospheres under physiological pH (7.2) was well correlated to the Langmuir-type adsorption equation. The electrostatic interactions between the protein molecules and those macrospheres well interpret the adsorption isotherms, while the mesopores in the Ca-SiO2 contributed to some extent. A multi-layer adsorption model was proposed.

Effect of Progesterone and Synthetic Progestins on Whole Blood Clot Formation and Erythrocyte Structure

2017 ◽  
Vol 23 (3) ◽  
pp. 607-617 ◽  
Author(s):  
Albe C. Swanepoel ◽  
Odette Emmerson ◽  
Etheresia Pretorius
Keyword(s):  
Whole Blood ◽  
Blood Clot ◽  
Thrombotic Event ◽  
Clot Formation ◽  
Erythrocyte Aggregation ◽  
Erythrocyte Morphology ◽  
Increased Risk ◽  
Blood Clots ◽  
Membrane Ultrastructure

AbstractCombined oral contraceptive (COC) use is a risk factor for venous thrombosis (VT) and related to the specific type of progestin used. VT is accompanied by inflammation and pathophysiological clot formation, that includes aberrant erythrocytes and fibrin(ogen) interactions. In this paper, we aim to determine the influence of progesterone and different synthetic progestins found in COCs on the viscoelasticity of whole blood clots, as well as erythrocyte morphology and membrane ultrastructure, in an in vitro laboratory study. Thromboelastography (TEG), light microscopy, and scanning electron microscopy were our chosen methods. Our results point out that progestins influence the rate of whole blood clot formation. Alterations to erythrocyte morphology and membrane ultrastructure suggest the presence of eryptosis. We also note increased rouleaux formation, erythrocyte aggregation, and spontaneous fibrin formation in whole blood which may explain the increased risk of VT associated with COC use. Although not all COC users will experience a thrombotic event, individuals with a thrombotic predisposition, due to inflammatory or hematological illness, should be closely monitored to prevent pathological thrombosis.

Role of factor XIII in fibrin clot formation and effects of genetic polymorphisms

Blood ◽  
2002 ◽  
Vol 100 (3) ◽  
pp. 743-754 ◽  
Author(s):  
Robert A. S. Ariëns ◽  
Thung-Shenq Lai ◽  
John W. Weisel ◽  
Charles S. Greenberg ◽  
Peter J. Grant
Keyword(s):  
Genetic Polymorphisms ◽  
Factor Xiii ◽  
Blood Clot ◽  
Site Directed Mutagenesis ◽  
Clot Formation ◽  
Factor Xiiia ◽  
Clotting Factors ◽  
Functional Features

Abstract Factor XIII and fibrinogen are unusual among clotting factors in that neither is a serine protease. Fibrin is the main protein constituent of the blood clot, which is stabilized by factor XIIIa through an amide or isopeptide bond that ligates adjacent fibrin monomers. Many of the structural and functional features of factor XIII and fibrin(ogen) have been elucidated by protein and gene analysis, site-directed mutagenesis, and x-ray crystallography. However, some of the molecular aspects involved in the complex processes of insoluble fibrin formation in vivo and in vitro remain unresolved. The findings of a relationship between fibrinogen, factor XIII, and cardiovascular or other thrombotic disorders have focused much attention on these 2 proteins. Of particular interest are associations between common variations in the genes of factor XIII and altered risk profiles for thrombosis. Although there is much debate regarding these observations, the implications for our understanding of clot formation and therapeutic intervention may be of major importance. In this review, we have summarized recent findings on the structure and function of factor XIII. This is followed by a review of the effects of genetic polymorphisms on protein structure/function and their relationship to disease.

Sign in / Sign up

Export Citation Format

Share Document