Antibody Immobilization onto Glow Discharge Treated Polymers

Safranj, Agneza; Kiaei, David; Hoffman, Allan S.

doi:10.1021/bp00008a012

Cited by 20 publications

(7 citation statements)

References 4 publications

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“…The fact that fluorocarbon RFGD treatment significantly influences protein adsorption and the state of adsorbed proteins has been reported in several studies [9,[15][16][17][18]. Previously, it was shown that RFGD fluorocarbon treatment decreased SDS elutability of surface-bound FGN when adsorbed from either pure FGN solution [16] or a FGN/γ -globulin mixture [9].…”

Section: The Influence Of Fluorocarbon Rfgd Treatments Of Pet On Fgn mentioning

confidence: 87%

Platelet adhesion to radiofrequency glow-discharge-deposited fluorocarbon polymers preadsorbed with selectively depleted plasmas show the primary role of fibrinogen

Tsai

Shi²,

Grunkemeier³

et al. 2004

Journal of Biomaterials Science, Polymer Edition

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Fluorocarbon radio-frequency glow-discharge (RFGD) treatment has previously been shown to cause decreased platelet adhesion despite the presence of adsorbed fibrinogen on the surfaces. In this study platelet adhesion to fluorocarbon RFGD-treated surfaces preadsorbed with human plasma was further examined. A series of plasma deposited fluorocarbon thin films were made by varying the C3F6/CH4 ratio in the monomer feed. The surfaces were preadsorbed with plasma, serum, or plasma selectively depleted of fibronectin, vitronectin, or Von Willebrand factor, and platelet adhesion was measured. We also measured fibrinogen adsorption to the surfaces from plasma, monoclonal antibody binding to adsorbed fibrinogen and SDS elutability of the adsorbed fibrinogen. The antibodies used bind to the three putative platelet binding sites on fibrinogen, namely, M1 antibody binds to the dodecapeptide at the C-terminus of the gamma chain, gamma (402-411), R1 antibody binds to a sequence in the Aalpha chain (87-100) which includes RGDF at Aalpha (95-98) and R2 antibody binds a sequence in the Aalpha chain (566-580) which includes RGDS at Aalpha (572-575). Fibrinogen was found to play a decisive role in mediating platelet adhesion to the fluorocarbon surfaces contacting plasma. Few platelets adhered to the fluorocarbon surfaces preadsorbed with serum, while preadsorption with plasma selectively-depleted of either fibronectin, vitronectin, or von Willebrand factor did not decrease platelet adhesion significantly. Replenishment of exogenous fibrinogen to serum restored platelet adhesion, while replenishment of the other proteins had no effect. Platelet adhesion to the fluorocarbon surfaces was lower than to PET or the methane glow-discharge-treated PET. However, there was no apparent correlation between platelet adhesion and the amount of fibrinogen adsorption or monoclonal antibody binding to surface-bound fibrinogen.

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Section: The Influence Of Fluorocarbon Rfgd Treatments Of Pet On Fgn mentioning

confidence: 87%

Platelet adhesion to radiofrequency glow-discharge-deposited fluorocarbon polymers preadsorbed with selectively depleted plasmas show the primary role of fibrinogen

Tsai

Shi²,

Grunkemeier³

et al. 2004

Journal of Biomaterials Science, Polymer Edition

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“…Evidence for covalent attachment Strong protein attachment, resistant to SDS elution, was first reported to occur on plasma-deposited polymers in the early 1990s (Bohnert et al 1990;Safranj et al 1991;Kiaei et al 1992;Chen et al 1993;Danilich et al 1992). At that time, Kiaei et al attributed the strong attachment to physisorption due to strong hydrophobic interactions while Danilich et al attributed it to covalent bonding.…”

Section: Retention Of Activity After Freeze Dryingmentioning

confidence: 99%

Plasma modified surfaces for covalent immobilization of functional biomolecules in the absence of chemical linkers: towards better biosensors and a new generation of medical implants

2010

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Plasma modification and plasma polymer deposition are valuable technologies for the preparation of surfaces for the covalent binding of biomolecules for applications such as biosensors, medical prostheses, and diagnostic devices as well as surfaces for enzyme-mediated reactions. Covalency is conveniently tested by the ability of the surface to retain the attached molecules after vigorous washing with sodium dodecyl sulphate (SDS). Covalency is indicated if the fraction of protein retained lies above the curve characteristic of physisorption. Confidence in covalency is strengthened when the washing protocol is aggressive enough to remove all adsorbed protein from a control significantly more hydrophobic than the test surface. The use of linker chemistry to space the molecules from the surface is in some cases beneficial. However, the use of linker chemistry is not necessary to retain molecular function for long periods when the polymer surface is modified by energetic bombardment. The energetic bombardment retains hydrophilicity of the surface by crosslinking the subsurface, and this appears to facilitate retention of protein function. Energetic bombardment also increases the functional life of molecules immobilized and then freeze dried on plasma-modified surfaces. Analysis of the surfaces shows that the covalent binding mechanism is related to the presence of free radicals on the surface and in the subsurface regions. The unpaired electrons associated with the radicals appear to be mobile within the modified region and can diffuse to the surface to take part in binding interactions. Proactive implantable devices can make use of these principles of covalent attachment by seeding the surface of an implant with a biomolecule that elicits the desired interaction with cells and prevents undesirable responses.

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“…After polyethylene terephthalate (PET) film has been incubated with fibrinogen for 4 hours, more than 60% of the protein is resistant to SDS elution [56]. Albumin and IgG behave similarly [57]. A recent study employing grazing angle infrared analysis was conducted to determine the interactions of fibrinogen and albumin adsorption onto hydrophobic and hydrophilic surfaces.…”

Section: Introductionmentioning

confidence: 99%

Surface Chemistry Influences Implant Biocompatibility

Thevenot

Tang³

2008

CTMC

667

224

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Implantable medical devices are increasingly important in the practice of modern medicine. Unfortunately, almost all medical devices suffer to a different extent from adverse reactions, including inflammation, fibrosis, thrombosis and infection. To improve the safety and function of many types of medical implants, a major need exists for development of materials that evoked desired tissue responses. Because implant-associated protein adsorption and conformational changes thereafter have been shown to promote immune reactions, rigorous research efforts have been emphasized on the engineering of surface property (physical and chemical characteristics) to reduce protein adsorption and cell interactions and subsequently improve implant biocompatibility. This brief review is aimed to summarize the past efforts and our recent knowledge about the influence of surface functionality on protein:cell:biomaterial interactions. It is our belief that detailed understandings of bioactivity of surface functionality provide an easy, economic, and specific approach for the future rational design of implantable medical devices with desired tissue reactivity and, hopefully, wound healing capability.

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Antibody Immobilization onto Glow Discharge Treated Polymers

Cited by 20 publications

References 4 publications

Platelet adhesion to radiofrequency glow-discharge-deposited fluorocarbon polymers preadsorbed with selectively depleted plasmas show the primary role of fibrinogen

Platelet adhesion to radiofrequency glow-discharge-deposited fluorocarbon polymers preadsorbed with selectively depleted plasmas show the primary role of fibrinogen

Plasma modified surfaces for covalent immobilization of functional biomolecules in the absence of chemical linkers: towards better biosensors and a new generation of medical implants

Surface Chemistry Influences Implant Biocompatibility

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