While hydrophobic surfaces coated with the poly[ethylene oxide]-poly[propylene oxide]-poly[ethylene oxide] (PEO-PPO-PEO) surfactant Pluronic® F108 are highly resistant to plasma protein adsorption, the antimicrobial peptide nisin has been observed to adsorb in multilayer quantities at such surfaces, and the PEO chains themselves suggested to inhibit nisin exchange by blood proteins. But...
Infections in hospitals account for over 100,000 deaths per year. These infections occur at the
hospital from complications following bacterial adhesion to intravenous catheters, coronary
stents and other implanted devices. Another common problem is protein adsorption to the
surface of the device and subsequent blood clotting. Methods for combating these...
Contact of blood with the surfaces of synthetic materials is associated with spontaneous protein adsorption, initiating platelet aggregation, the coagulation cascade, and the eventual development of a stable clot. Current therapy to inhibit implant-induced thrombosis is life-long administration of systemic anticoagulants. An alternative to the systemic administration of anticoagulant drugs...
Passage of blood through a sorbent device for removal of bacteria and endotoxin by specific binding with immobilized, membrane-active, bactericidal peptides holds promise for treating severe blood infections. Peptide insertion in the target membrane and stable binding is desirable, while membrane disruption and release of degradation products to the circulating...
Nisin, an amphiphilic, antimicrobial peptide, has been shown to integrate into the hydrophobic inner region of poly(ethylene oxide) (PEO) brush layers; however, the presence of integrated nisin may compromise the protein repulsive character of the PEO layer. In particular, the introduction of fibrinogen to nisin-loaded brush layers has been observed...
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Joseph McGuire
Nisin, an amphiphilic, antimicrobial peptide, has been shown to integrate
Nisin, an antibacterial peptide proven to be an effective inhibitor of Gram-positive bacteria, was incorporated into novel block copolymer constructs and tested for retained antibacterial activity. Covalent coupling was achieved by chemical modification of the N-terminal isoleucine to introduce a thiol group. Thiolated nisin derivatives were then linked to poly[ethylene...
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Joseph McGuire
Nisin, an antibacterial peptide proven to be an effective inhibitor of Gram
Adsorption kinetic data recorded for α-lactalbumin, β-casein, β-lactoglobulin, bovine serum albumin and lysozyme at silianized silica surfaces of low and high hydrophobicity, along with a simple model for adsorption and surfactant-mediated elution of protein, were used to analyze the removal of each protein by sodium dodecylsulfate (SDS) and dodecyltrimethylammonium bromide...
Nisin is an antibacterial peptide, which when adsorbed
on a surface can inhibit bacterial adhesion and viability.
The ability of noncovalently immobilized nisin to withstand
exchange by the milk proteins bovine serum albumin, β-lactoglobulin, α-lactalbumin, and β-casein on surfaces that
had been silanized with dichlorodiethylsilane to exhibit
high and low...