PubMed Health⌕ Search

PubMed · 11835169

Fluorinated surface-modifying macromolecules: modulating adhesive protein and platelet interactions on a polyether-urethane.

Abstract

Polyether-urethanes (PEUs) have been the materials of choice for the manufacture of conventional blood-contacting devices. Nevertheless, biostability and blood compatibility are still among the principal limitations in their long-term application. Studies investigating the development of protective coatings for PEUs have shown that degradation can be reduced with the use of fluorinated surface-modifying macromolecules (SMMs). It has also been hypothesized that SMM-modified PEU surfaces may exhibit improved blood compatibility because other studies have shown a modulation in fibrinogen adsorption onto these surfaces. To determine the blood compatibility of a PEU-containing fluorinated SMMs, a series of in vitro experiments were designed to study the pattern of protein adsorption from plasma and then to assess the nature of platelet adhesion and activation on each substrate. Western blot analysis as well as single protein studies revealed that the dominant "adhesive proteins" [fibrinogen (Fg), fibronectin (Fnc), and vitronectin (Vnc)] were adsorbed on two of the SMM-containing PEUs in lower amounts relative to unmodified base. Platelet adhesion and activation data further highlighted the differences among the various substrates. It was shown that the unmodified base had a higher number of adhered platelets relative to the SMM-modified surfaces, and that of the SMM-containing substrates, which showed the lowest levels of adhesive proteins also, exhibited significantly lower platelet densities. Close morphological examination further revealed that platelets residing on these latter substrates were not appreciably activated. Based on the current evidence, it is believed that the fluorinated SMMs demonstrate good potential for the development of surfaces with minimal thrombogenic character in in vivo applications.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

A R Jahangir, W G McClung, R M Cornelius, C B McCloskey, J L Brash, J P Santerre. 2002. Fluorinated surface-modifying macromolecules: modulating adhesive protein and platelet interactions on a polyether-urethane.. https://doi.org/10.1002/jbm.10033

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

Three-dimensional porous nano-hydroxyapatite@gelatin composite as efficient adsorbent for uranyl ion removal from low-level radioactive wastewater.

The contamination of water resources by uranyl (UO22+) ions poses significant environmental and health risks, requiring the development of efficient and sustainable remediation strategies. Adsorption-based techniques have emerged as promising approaches in the field of UO22+ removal, but the design of cost-effective, high-capacity, and environmentally friendly adsorbents remains challenging. In this study, a three-dimensional porous nano-hydroxyapatite@gelatin (nHAP@Ge) composite was synthesized through glutaraldehyde cross-linking, combining the structural stability of Ge with the high uranium affinity of nHAP. The optimized nHAP@Ge, with a nHAP:Ge mass ratio of 1:0.5, exhibited exceptional UO22+ removal efficiency (97 %), along with high adsorption capacity (364.03 mg/g). Systematic characterizations using scanning electron microscopy (SEM), thermogravimetric analysis (TGA), Fourier transform infrared (FT-IR) spectroscopy, and X-ray photoelectron spectroscopy (XPS) methods revealed that the porous structure and surface functional groups (-OH, Ca2+, and PO43-) of the material synergistically contributed to binding UO22+ species. Furthermore, the incorporation of nHAP into the Ge framework resulted in enhanced thermal stability while significantly improving the UO22+ adsorption performance. This work presents a scalable, eco-friendly, and recyclable strategy for the effective treatment of uranium-contaminated water, with potential applications in nuclear wastewater treatment and environmental remediation.

Adsorption↗

Dual radiolabeling to study protein adsorption competition in relation with hemocompatibility.

Human fibrinogen (Fg) and albumin (HSA) were labeled with (3)H and (14)C, respectively. Dual counting allowed the adsorbed amount of the two proteins to be determined simultaneously. Single adsorption, adsorption of the two proteins in competition, but also exchange (substitution by molecules of the same nature) and displacement (desorption under the action of the other protein) experiments were performed on two model surfaces, glass and polystyrene (PS), as well as on pure polyvinylchloride (PVC-s) and on PVC from blood bag (PVC-b). As expected, the adsorbed amount of a single protein is higher on a hydrophobic compared to a hydrophilic surface. When the two proteins are adsorbed in competition, they are found in equal proportion on glass, while HSA is twice more abundant than Fg on PS and PVC-s and about six times more abundant on PVC-b. This trend is related to an increase of the water contact angle of the substrates. For PVC-b, the contact angle is affected by the presence of aliphatic components exposed at the extreme surface, as determined by angle-resolved X-ray photoelectron spectroscopy. In exchange and displacement experiments, the first adsorbed molecules remain dominating on PS while they can be removed from glass. Given the known importance of HSA and Fg adsorption for the fate of materials placed in contact with blood, the method described in this paper may be used as a first approach to orient the design of surfaces with improved hemocompatibility.

Adsorption↗

Effective immobilization of subunit protein in mesoporous silica modified with ethanol.

Ethoxylated FSM-type mesoporous silica (folded-sheet mesoporous material) with a pore diameter of 6.2 nm (FSM6.2) remarkably enhances rigidly of the structure in aqueous solutions. The esterified material could be used successfully as an adsorbent to accommodate subunit protein, methemoglobin (Fe(3+)). Furthermore, methemoglobin (Fe(3+)) in the pores of ethoxy-FSM is maintained a peroxidase activity similar to the native, indicating methemoglobin retains its fore subunit structure in the pores of FSM6.2.

Adsorption↗