Acetylene plasma polymerized surfaces for covalent immobilization of dense bioactive protein monolayers

Yin, Y.; Bilek, Marcela M.M.; McKenzie, David R.; Nosworthy, Neil J.; Kondyurin, Alexey; Youssef, Hani; Byrom, Michael; Yang, Wenrong

doi:10.1016/j.surfcoat.2008.10.035

Cited by 50 publications

(28 citation statements)

References 23 publications

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“…The plasma polymers and plasma-modified surfaces created using energetic ion bombardment reported more recently are even more hydrophilic (Yin et al 2009e;Kondyurin et al 2009b) than the most hydrophilic surface studied in the earlier works, but nevertheless show much higher levels of SDS-resistant protein attachment (see, for example, MacDonald et al 2008;Yin et al 2009d;Nosworthy et al 2007;Kondyurin et al 2008b, c;Bax et al 2009), rivalling those observed on the most hydrophobic of surfaces examined in the earlier studies. Figure 4 shows where the data obtained on the energetic ion-treated surfaces lie in relation to the adsorption curve of Kiaei et al (1992).…”

Section: Retention Of Activity After Freeze Dryingmentioning

confidence: 67%

“…A quartz crystal microbalance was used to observe the kinetics of attachment onto acetylene plasmapolymerized layers. The masses of catalase and HRP bound in an SDS-resistant manner corresponded to a dense monolayer coverage (Yin et al 2009d). …”

Section: Attachment Of Dense Protein Monolayersmentioning

confidence: 99%

“…These data are indicative of the existence of a mechanism other than physisorption for attachment to plasma deposited and modified polymers which may also account for the outlier in the earlier data of Kiaei et al Also shown is a point representing an untreated PTFE control used in the later works, which is also well away from the curve. The mechanism invoked to explain the deviations from the curve is the formation of a covalent bond between an active group on the surface and an exposed side chain of the protein (Bax et al 2009;Yin et al 2009d). This interpretation is supported by the use of a more aggressive SDS washing protocol in which the SDS (1-2% w/v) solution was heated to 70-90°C.…”

Section: Retention Of Activity After Freeze Dryingmentioning

confidence: 99%

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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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Section: Retention Of Activity After Freeze Dryingmentioning

confidence: 67%

Section: Attachment Of Dense Protein Monolayersmentioning

confidence: 99%

Section: Retention Of Activity After Freeze Dryingmentioning

confidence: 99%

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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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“…SDS denatures secondary and non-sulphide-linked tertiary structures of proteins and is used widely in biochemistry, especially in SDS-PAGE gels to separate proteins. The SDS washing protocol used in this paper satisfies the conditions established in previous studies [18,20,21] to test for the covalent attachment of proteins to surfaces. SDS breaks non-covalent interactions between proteins and the surface, unfolding proteins and releasing them to the solution.…”

Section: Characterization Of Yeast Cell Residuesmentioning

confidence: 99%

Ion-implanted polytetrafluoroethylene enhances Saccharomyces cerevisiae biofilm formation for improved immobilization

Tran

Kondyurin

Hirsh

et al. 2012

J. R. Soc. Interface.

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The surface of polytetrafluoroethylene (PTFE) was modified using plasma immersion ion implantation (PIII) with the aim of improving its ability to immobilize yeast. The density of immobilized cells on PIII-treated and -untreated PTFE was compared as a function of incubation time over 24 h. Rehydrated yeast cells attached to the PIII-treated PTFE surface more rapidly, with higher density, and greater attachment strength than on the untreated surface. The immobilized yeast cells were removed mechanically or chemically with sodium hydroxide and the residues left on the surfaces were analysed with Fourier transform infrared spectroscopy-attenuated total reflection (FTIR-ATR) and X-ray photoelectron spectroscopy (XPS). The results revealed that the mechanism of cell attachment on both surfaces differs and a model is presented for each. Rapid attachment on the PIII-treated surface occurs through covalent bonds of cell wall proteins and the radicals on the treated surface. In contrast, on the untreated surface, only physisorbed molecules were found in the residue and lipids were more highly concentrated than proteins. The presence of lipids in the residue was found to be a consequence of damage to the plasma membrane during the rehydration process and the increased cell stress was also apparent by the amount of Hsp12 in the protein residue. The immobilized yeast cells on PIII-treated PTFE were found to be as active as yeast cells in suspension.

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“…An effective method of creating buried radicals is to treat an organic polymer with energetic ions (13,14). After treatment with energetic ions, either postformation or during their deposition, these surfaces strongly immobilize proteins (15)(16)(17)(18)(19)(20)(21)(22)(23)(24)(25)(26)(27)(28)(29) and provide a means of cloaking biomaterial surfaces. What is required is a means of controlling the density of radicals to bind a full protein monolayer that is not compromised by excessive numbers of covalent bonds, while giving sufficient shelf life of the binding property for practical applications.…”

mentioning

confidence: 99%

Free radical functionalization of surfaces to prevent adverse responses to biomedical devices

Bilek

Bax

Kondyurin

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

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189

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Immobilizing a protein, that is fully compatible with the patient, on the surface of a biomedical device should make it possible to avoid adverse responses such as inflammation, rejection, or excessive fibrosis. A surface that strongly binds and does not denature the compatible protein is required. Hydrophilic surfaces do not induce denaturation of immobilized protein but exhibit a low binding affinity for protein. Here, we describe an energetic ion-assisted plasma process that can make any surface hydrophilic and at the same time enable it to covalently immobilize functional biological molecules. We show that the modification creates free radicals that migrate to the surface from a reservoir beneath. When they reach the surface, the radicals form covalent bonds with biomolecules. The kinetics and number densities of protein molecules in solution and free radicals in the reservoir control the time required to form a full protein monolayer that is covalently bound. The shelf life of the covalent binding capability is governed by the initial density of free radicals and the depth of the reservoir. We show that the high reactivity of the radicals renders the binding universal across all biological macromolecules. Because the free radical reservoir can be created on any solid material, this approach can be used in medical applications ranging from cardiovascular stents to heart-lung machines.

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Acetylene plasma polymerized surfaces for covalent immobilization of dense bioactive protein monolayers

Cited by 50 publications

References 23 publications

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

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

Ion-implanted polytetrafluoroethylene enhances Saccharomyces cerevisiae biofilm formation for improved immobilization

Free radical functionalization of surfaces to prevent adverse responses to biomedical devices

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