Effect of single-chain and two-chain high molecular weight kininogen on adsorption of fibrinogen from binary mixtures to glass and sulfonated polyurethane surfaces

Cornelius, Rena M.; Brash, John L.

doi:10.1002/(sici)1097-4636(19971205)37:3<314::aid-jbm2>3.0.co;2-o

Cited by 17 publications

(2 citation statements)

References 31 publications

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“…The outcome of the competitive behaviour onto the SCA surface has been previously observed using other proteins. Brash's group (Cornelius & Brash 1997) showed a significant reduction in fibrinogen adsorption on different surfaces when high-molecular-weight kininogen was co-adsorbed. In this study, results indicated that the presence of HSA had a negative effect on the level of adsorbed HFN.…”

Section: Protein Behaviour In Competitive Conditions: Binary Systemsmentioning

confidence: 99%

The competitive adsorption of human proteins onto natural-based biomaterials

Alves

Reis

Hunt

2010

J. R. Soc. Interface.

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This study aims to further the understanding of nanoscale structures relevant for cellular recognition on contact and interaction with natural-based materials. The correlation between surface characteristics and protein adsorption from unitary and complex protein systems was investigated with respect to altering the bulk chemistry of the substrate material. Polymeric blends of starch and cellulose acetate, polycaprolactone (SPCL) and ethylene vinyl alcohol (SEVA-C) were used. Different proteins, bovine serum albumin, human serum albumin (HSA) and human fibronectin (HFN), were selected for this study. The construction of adsorption isotherms is an important starting point towards characterizing the interactions between surfaces and proteins. In this study, albumin adsorption isotherms fit the Freundlich model and were correlated with the chemistry and morphology of surfaces. In addition, protein distribution, quantification and competition were measured using fluorimetry and visualized by confocal microscopy. The analysis of unitary systems demonstrated that the adsorption of HSA was generally lower than that of HFN. In the latter case, SPCL and SEVA-C blends reached adsorption values of 97 and 89 per cent, respectively. In studying the co-adsorption of proteins, an increase in both HSA and HFN on SEVA-C surfaces was observed. SPCL showed no substantial increase in the adsorption of the proteins in competitive conditions. The similarity of these materials with other polysaccharide-based materials increases the relevance of the presented results. This study provides valuable information for the development of strategies towards the control of protein orientation and functionality as the availability of cell signalling epitopes for a broader family of materials that continue to be a significant component of this field of research.

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Section: Protein Behaviour In Competitive Conditions: Binary Systemsmentioning

confidence: 99%

The competitive adsorption of human proteins onto natural-based biomaterials

Alves

Reis

Hunt

2010

J. R. Soc. Interface.

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show abstract

“…There are two possible explanations of this apparent discrepancy. First, the findings of Cornelius and Brash suggest that SC-HMWK undergoes a conformational transformation to DC-HMWK during the course of protein adsorption onto surfaces, 36 which also may have occurred under our culture conditions. Second, our SDS-PAGE results indicate the possible contamination of commercially obtained SC-HMWK by DC-HMWK (Fig.…”

Section: Discussionmentioning

confidence: 89%

High molecular weight kininogen inhibition of endothelial cell function on biomaterials

Voskerician

Anderson

Ziats

2000

J. Biomed. Mater. Res.

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Synthetic vascular grafts implanted into humans fail to develop a complete endothelial lining. In previous studies, we have shown that high-molecular-weight kininogens (HMWK) adsorb to the surfaces of biomaterials. In addition, it has been demonstrated that these proteins modulate cellular function. In the present study, we report on the adhesion and proliferation of human umbilical-vein endothelial cells (HUVEC) on tissue culture polystyrene, glass, polyurethane, and Mylar(trade mark) surfaces coated with human HMWK, either single-chain HMWK (SC-HMWK) or double-chain HMWK (DC-HMWK). Surfaces coated with fibronectin served as a positive control for these experiments. Parallel experiments were performed in which HUVEC were allowed to migrate from crosslinked dextran microcarrier beads (Cytodex 2) onto HMWK-coated surfaces. Our results indicate that HMWK-coated surfaces inhibit endothelial cell adhesion, proliferation, and migration at 24 and 72 h, and this inhibition is concentration dependent. To determine a potential mechanism for this inhibitory phenomenon, cells were stained for cytoskeletal actin filaments using rhodamine-phalloidin. Endothelial cells on HMWK-coated surfaces displayed F-actin filament reorganization/disassembly, characterized by the absence of peripheral actin bands in focal adhesion contacts. We conclude that HMWK inhibit endothelial cell adhesion, proliferation, and migration on a variety of biomaterial surfaces. This inhibitory effect may play a role in promoting the lack of endothelialization in synthetic vascular grafts, which is thought to play a significant role in the failure of these devices.

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Peptide modified gold-coated polyurethanes as thrombin scavenging surfaces

Sun

Sheardown

Tengvall

et al. 2000

J. Biomed. Mater. Res.

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Thin layers of gold were deposited on polyurethane film and chemisorbed with three peptides having an N-terminal cysteine: Cys-Pro-Arg, Cys-(L)Phe-Pro-Arg, and Cys-(D)Phe-Pro-Arg. The ability of these surfaces to act as thrombin scavengers was evaluated. The peptides are related to the known thrombin inhibitor Phe-Pro-Arg chloromethyl ketone and were shown to have significant thrombin inhibitory activity in solution. Attachment of the peptides to gold was confirmed by water contact angle and X-ray photoelectron spectroscopy measurements. Thrombin adsorption from a buffer and plasma was investigated, and chromogenic substrate assays were carried out for thrombin activity on the surfaces and in the supernatant following adsorption. The data suggest that the peptide-modified surfaces are able to adsorb thrombin with high affinity from a buffer and that thrombin is taken up selectively from plasma. The Cys-(D)Phe-Pro-Arg modified surfaces showed particularly high affinity for thrombin. It was also found that the activity of thrombin adsorbed on the peptide surfaces was inhibited, and inhibition was greatest on the Cys-(D)Phe-Pro-Arg surface. We concluded that the peptide surfaces may have potential as antithrombogenic materials via their ability to scavenge and inhibit thrombin generated as a result of blood-material contact.

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Effect of single-chain and two-chain high molecular weight kininogen on adsorption of fibrinogen from binary mixtures to glass and sulfonated polyurethane surfaces

Cited by 17 publications

References 31 publications

The competitive adsorption of human proteins onto natural-based biomaterials

The competitive adsorption of human proteins onto natural-based biomaterials

High molecular weight kininogen inhibition of endothelial cell function on biomaterials

Peptide modified gold-coated polyurethanes as thrombin scavenging surfaces

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