Reduction of fibrinogen adsorption on PEG‐coated polystyrene surfaces

Bergström, Karin; Holmberg, Krister; Safranj, Agneza; Hoffman, Allan S.; Edgell, M. J.; Kozlowski, Antoni; Hovanes, Bruce A.; Harris, J. Milton

doi:10.1002/jbm.820260607

Cited by 191 publications

(112 citation statements)

References 18 publications

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“…It can be noted that the polymers evaluated in this study all accumulate proteins, in contrast to nonadsorbing "stealth" surfaces based on neutral or zwitterionic polymers such as poly(ethylene oxide) and poly(carboxybetaine methacrylate). [43][44][45][46][47] Considering the in vivo situation, the soft PLMA surface will become covered with proteins, but as indicated in our study, in a rather native conformation. In contrast, a poly(ethylene glycol) modified surface will be free from proteins.…”

Section: D417-5 Fromellmentioning

confidence: 99%

Absence of conformational change in complement factor 3 and factor XII adsorbed to acrylate polymers is related to a high degree of polymer backbone flexibility

et al. 2017

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In previous investigations, the authors have examined the adsorption of albumin, immunoglobulin, and fibrinogen to a series of acrylate polymers with different backbone and side-group flexibility. The authors showed that protein adsorption to acrylates with high flexibility, such as poly(lauryl methacrylate) (PLMA), tends to preserve native conformation. In the present study, the authors have continued this work by examining the conformational changes that occur during the binding of complement factor 3 (C3) and coagulation factor XII (FXII). Native C3 adsorbed readily to all solid surfaces tested, including a series of acrylate surfaces of varying backbone flexibility. However, a monoclonal antibody recognizing a “hidden” epitope of C3 (only exposed during C3 activation or denaturation) bound to the C3 on the rigid acrylate surfaces or on polystyrene (also rigid), but not to C3 on the flexible PLMA, indicating that varying degrees of conformational change had occurred with binding to different surfaces. Similarly, FXII was activated only on the rigid poly(butyl methacrylate) surface, as assessed by the formation of FXIIa-antithrombin (AT) complexes; in contrast, it remained in its native form on the flexible PLMA surface. The authors also found that water wettability hysteresis, defined as the difference between the advancing and receding contact angles, was highest for the PLMA surface, indicating that a dynamic change in the interface polymer structure may help protect the adsorbed protein from conformational changes and denaturation.

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Section: D417-5 Fromellmentioning

confidence: 99%

Absence of conformational change in complement factor 3 and factor XII adsorbed to acrylate polymers is related to a high degree of polymer backbone flexibility

et al. 2017

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“…It has long been established that attachment of PEG to a solid surface inhibits protein adsorption (Bergström et al, 1992;Cheng et al, 1987;Jiang et al, 2003;Szleifer and Carignano, 2000). In this vein, Jeong and co-workers have observed that the extent of protein adsorption to co-polymer blends of PLG and PEG depends upon the PEG molecular weight (Jeong et al, 2000).…”

Section: Introductionmentioning

confidence: 96%

Adsorption of poly(ethylene glycol)‐modified ribonuclease A to a poly(lactide‐co‐glycolide) surface

Daly¹,

Przybycien²,

Tilton³

2005

Biotech & Bioengineering

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Protein adsorption is a source of variability in the release profiles of therapeutic proteins from biodegradable microspheres. We employ optical reflectometry and total internal reflection fluorescence to explore the extent and kinetics of ribonuclease A (RNase A) adsorption to spin-cast films of poly(lactide-co-glycolide) (PLG) and, in particular, to determine how covalent grafting of polyethylene glycol (PEG) to RNase A affects adsorption. Adsorption kinetics on PLG surfaces are surface-limited for RNase A but transport-limited for unconjugated PEG homopolymers and for PEG-modified RNase A, indicating that PEG anchors the conjugates to the surface during the transport-limited regime. PEG modification of RNase A decreases the total number of adsorbed molecules per unit area but increases the areal surface coverage because the grafted PEG chains exclude additional surface area. Total internal reflection fluorescence-based exchange measurements show that there is no exchange between adsorbed and solution-phase protein molecules. This indicates an unusually tenacious adsorption. Streaming current measurements indicate that the zeta potential of the PLG surface becomes increasingly negative as the film is exposed to water for several weeks, as expected. Aging of the PLG surface results in increased adsorption of unmodified RNase A but decreased adsorption of unconjugated PEG homopolymers and of PEG-RNase A conjugates, relative to the extent of adsorption on freshly prepared PLG surfaces. Adsorption results correlate well with an increase in the rate, total extent and preservation of bioactivity of RNase A released from PLG microspheres for the PEG-modified version of RNase A.

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“…PEG is widely recognized for its lack of interactions with macromolecules found in body fluids. [47][48][49] Use of PEG as a spacer arm or tether has been shown to increase the activity of bound enzymes. D'Urso et al 50 found that the K m of enzymes bound to a surface by a PEG tether is increased 10 -20 times over that of the native enzyme.…”

Section: Introductionmentioning

confidence: 99%

Corneal epithelial cell growth over tethered‐protein/peptide surface‐modified hydrogels

Jacob

Rochefort

et al. 2004

J Biomed Mater Res

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In this study, we investigated the corneal epithelial cell growth rate and adhesion to novel hydrogels with (1) extracellular matrix proteins [fibronectin, laminin, substance P, and insulin-like growth factor-1 (IGF-1)] and (2) peptide sequences [RGD and fibronectin adhesion-promoting peptide (FAP)] tethered to their surface on poly(ethylene glycol) (PEG) chains. The growth rate to confluence of primary rabbit cornea epithelial cells was compared for plain polymethacrylic acid-co-hydroxyethyl methacrylate (PHEMA/MAA) hydrogels, PHEMA/MAA hydrogels coated with extracellular matrix proteins or peptides, and PHEMA/ MAA hydrogels with tethered extracellular matrix proteins or peptides on the surface. The development of focal adhesions by the epithelial cells grown on the surfaces was determined by F-actin staining. Little to no epithelial cell growth occurred on the plain hydrogel surfaces throughout the 15-day culture period. Of the coated hydrogels, only the fibronectin-coated surfaces showed a significant increase in cell growth compared to plain hydrogels (p < 0.009). However, even these surfaces reached a maximum of only 20% confluence. Laminin, fibronectin adhesion-promoting peptide (FAP), and fibronectin/laminin (1:1) tether-modified hydrogels all achieved 100% confluence by the end of the culture period, although the rates at which confluence was reached differed. F-actin staining showed that focal adhesions were formed for the laminin, FAP, and fibronectin/laminin tether-modified surfaces. The results support the hypothesis that tethering certain extracellular matrix proteins and/or peptides to the hydrogel surface enhances epithelial cell growth and adhesion, compared with that seen for proteincoated or plain hydrogel surfaces.

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Reduction of fibrinogen adsorption on PEG‐coated polystyrene surfaces

Cited by 191 publications

References 18 publications

Absence of conformational change in complement factor 3 and factor XII adsorbed to acrylate polymers is related to a high degree of polymer backbone flexibility

Absence of conformational change in complement factor 3 and factor XII adsorbed to acrylate polymers is related to a high degree of polymer backbone flexibility

Adsorption of poly(ethylene glycol)‐modified ribonuclease A to a poly(lactide‐co‐glycolide) surface

Corneal epithelial cell growth over tethered‐protein/peptide surface‐modified hydrogels

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