Online citations, reference lists, and bibliographies.
Please confirm you are human
(Sign Up for free to never see this)
← Back to Search

Polyethylene Oxide Surfaces Of Variable Chain Density By Chemisorption Of PEO-thiol On Gold: Adsorption Of Proteins From Plasma Studied By Radiolabelling And Immunoblotting.

L. Unsworth, H. Sheardown, J. Brash
Published 2005 · Chemistry, Medicine

Save to my Library
Download PDF
Analyze on Scholarcy
Share
The mechanisms involved in the inhibition of protein adsorption by polyethylene oxide (PEO) are not completely understood, but it is believed that PEO chain length, chain density and chain conformation all play a role. In this work, surfaces formed by chemisorption of PEO-thiol to gold were investigated: the effects of PEO chain density, chain length (600, 750, 2000 and 5000 MW) and end-group (-OH, -OCH3) on protein adsorption from plasma are reported. Similar to previous single protein adsorption studies (L.D. Unsworth et al., Langmuir 2005;21:1036-41) it was found that, of the different surfaces investigated, PEO layers formed from solutions near the cloud point adsorbed the lowest amount of fibrinogen from plasma. Layers of hydroxyl-terminated PEO of MW 600 formed under these low solubility conditions showed almost complete suppression (versus controls) of the Vroman effect, with 20+/-1 ng/cm2 adsorbed fibrinogen at the Vroman peak and 6.7+/-0.6 ng/cm2 at higher plasma concentration. By comparison, Vroman peak adsorption was 70+/-20 and 50+/-3 ng/cm2, respectively, for 750-OCH3 and 2000-OCH3 layers formed under low solubility conditions; adsorption on these surfaces at higher plasma concentration was 16+/-9 and 12+/-3 ng/cm2. Thus in addition to the effect of solution conditions noted previously, the results of this study also suggest a chain end group effect which inhibits fibrinogen adsorption to, and/or facilitates displacement from, hydroxyl terminated PEO layers. Fibrinogen adsorption from plasma was not significantly different for surfaces prepared with PEO of molecular weight 750 and 2000 when the chain density was the same ( approximately 0.5 chains/nm2) supporting the conclusion that chain density may be the key property for suppression of protein adsorption. The proteins eluted from the surfaces after contact with plasma were investigated by SDS-PAGE and immunoblotting. A number of proteins were detected on the various surfaces including fibrinogen, albumin, C3 and apolipoprotein A-I. The blot responses were zero or weak for all four proteins of the contact system; some complement activation was observed on all of the surfaces studied.
This paper references
10.1051/JPHYS:01977003808098300
Adsorption of chain molecules with a polar head a scaling description
S. Alexander (1977)
10.1021/JA00351A063
ADSORPTION OF BIFUNCTIONAL ORGANIC DISULFIDES ON GOLD SURFACES
R. Nuzzo (1983)
10.1021/BK-1995-0602
Proteins at Interfaces II: Fundamentals and Applications
T. Horbett (1995)
10.1002/1097-4636(20010905)56:3<406::AID-JBM1110>3.0.CO;2-R
Chain-length dependence of the protein and cell resistance of oligo(ethylene glycol)-terminated self-assembled monolayers on gold.
B. Zhu (2001)
10.1002/APP.12545
Synthesis and characterization of thiol‐terminated poly(ethylene oxide) for chemisorption to gold surface
Y. J. Du (2003)
10.1002/1097-4636(20010905)56:3<324::AID-JBM1100>3.0.CO;2-P
Modification of Si(100) surface by the grafting of poly(ethylene glycol) for reduction in protein adsorption and platelet adhesion.
F. Zhang (2001)
10.1016/S0006-3495(97)78698-3
Protein adsorption on surfaces with grafted polymers: a theoretical approach.
I. Szleifer (1997)
10.1163/156856299X00667
Water and the acute biological response to surfaces.
E. Vogler (1999)
10.1163/156856201300194252
Modification of gold surface by grafting of poly(ethylene glycol) for reduction in protein adsorption and platelet adhesion
F. Zhang (2001)
10.1002/JBM.10048
Platelet adhesion to polystyrene-based surfaces preadsorbed with plasmas selectively depleted in fibrinogen, fibronectin, vitronectin, or von Willebrand's factor.
Wei-Bor Tsai (2002)
10.1016/0021-9797(86)90048-2
Phenomenology and mechanism of the transient adsorption of fibrinogen from plasma (Vroman effect)
P. Wojciechowski (1986)
10.1021/LA036027O
Influence of the thiol position on the attachment and subsequent hybridization of thiolated DNA on gold surfaces.
R. Wirtz (2004)
10.1021/JA00076A032
Adsorption of proteins onto surfaces containing end-attached oligo(ethylene oxide): a model system using self-assembled monolayers
K. Prime (1993)
Lipids and Lipoproteins in Clinical Practice
N. Mcintyre (1991)
10.1021/BK-1995-0602.CH008
The Vroman Effect: A Critical Review
S. M. Slack (1995)
10.1163/156856200743869
On the molecular basis of fouling resistance
M. Morra (2000)
10.1111/j.1749-6632.1987.tb33043.x
The Fate of Fibrinogen following Adsorption at the Blood‐Biomaterial, Interface a
J. Brash (1987)
10.1055/S-2007-1003477
The importance of surfaces in contact phase reactions.
L. Vroman (1987)
10.1016/0267-6605(93)90017-2
Complement activation and cytokine production as consequences of immunological bioincompatibility of extracorporeal circuits.
G. Jahns (1993)
10.1163/156856293X00573
Identification of proteins absorbed to hemodialyser membranes from heparinized plasma.
R. Cornelius (1993)
10.1055/S-0038-1661093
Effect of plasma dilution on adsorption of fibrinogen to solid surfaces.
J. Brash (1984)
10.1016/J.JCIS.2004.08.022
Chemisorption of thiolated poly(ethylene oxide) to gold: surface chain densities measured by ellipsometry and neutron reflectometry.
L. Unsworth (2005)
10.1021/BI00107A001
The coagulation cascade: initiation, maintenance, and regulation.
E. Davie (1991)
10.1016/S0142-9612(01)00334-9
Effects of cloud-point grafting, chain length, and density of PEG layers on competitive adsorption of ocular proteins.
P. Kingshott (2002)
10.1002/JBM.10117
Adsorption of proteins from infant and adult plasma to biomaterial surfaces.
R. Cornelius (2002)
Poly(Ethylene Glycol) Chemistry Biotechnical and Biomedical Applications
J. M. Harris (1992)
10.1006/JCIS.1998.5513
Effect of chain density on inhibition of protein adsorption by poly(ethylene glycol) based coatings
Martin Malmsten (1998)
10.1007/978-1-4684-8610-0
Surface and Interfacial Aspects of Biomedical Polymers
J. Andrade (1985)
10.1016/S1359-0286(99)00018-2
Surfaces that resist bioadhesion
P. Kingshott (1999)
10.1016/S0142-9612(02)00083-2
Identification of apolipoprotein A-I as a major adsorbate on biomaterial surfaces after blood or plasma contact.
R. Cornelius (2002)
10.1163/156856200744345
Poly(ethylene glycol): Protein-repulsive or albumin-compatible?
M. Vert (2000)
10.1016/S0927-7765(99)00053-3
Measurement of protein adsorption to gold surface by radioiodination methods: suppression of free iodide sorption
Y. J. Du (2000)
10.1021/LA047672D
Protein resistance of surfaces prepared by sorption of end-thiolated poly(ethylene glycol) to gold: effect of surface chain density.
L. Unsworth (2005)



This paper is referenced by
10.1007/s10118-012-1118-2
Poly(N-vinylpyrrolidone)-modified surfaces repel plasma protein adsorption
Xiaoli Liu (2012)
10.4315/0362-028X.JFP-14-042
Activity retention after nisin entrapment in a polyethylene oxide brush layer.
Julie A. Auxier (2014)
10.1155/2012/584060
BSA Nanoparticles for siRNA Delivery: Coating Effects on Nanoparticle Properties, Plasma Protein Adsorption, and In Vitro siRNA Delivery
Haran Yogasundaram (2012)
Integrin- mediated interactions between cells and biomimetic materials. Physical Measurements of Single Biomolecules: Experiment and Simulation
R. Knerr (2003)
10.1039/C5TB00732A
Star-shaped poly(2-methyl-2-oxazoline)-based films: rapid preparation and effects of polymer architecture on antifouling properties.
C. Zhang (2015)
10.1016/j.actbio.2010.02.043
Surface modification with an antithrombin-heparin complex for anticoagulation: studies on a model surface with gold as substrate.
K. Sask (2010)
Host responses to microgel-based biomaterial interfaces
A. Bridges (2008)
10.1016/j.actbio.2014.09.010
Protein adsorption can be reversibly switched on and off on mixed PEO/PAA brushes.
M. Delcroix (2015)
10.1134/S1061933X15040183
Conjugates of gold nanoparticles and poly(ethylene glycol): Formation in hydrosol, direct transfer to organic medium, and stability of organosols
V. Terekhin (2015)
10.1163/092050610X508400
Application of MS-Based Proteomics to Study Serum Protein Adsorption/Absorption and Complement C3 Activation on Poly(ethylene glycol) Hydrogels
X. Wang (2011)
10.1002/mabi.201000223
Inhibitory effect of hydrophilic polymer brushes on surface-induced platelet activation and adhesion.
Y. Zou (2010)
10.1002/jbm.a.34218
Polyurethane modified with an antithrombin-heparin complex via polyethylene oxide linker/spacers: influence of PEO molecular weight and PEO-ATH bond on catalytic and direct anticoagulant functions.
K. Sask (2012)
10.1039/C2JM15814K
Preparation of antibacterial surfaces by hyperthermal hydrogen induced cross-linking of polymer thin films
Solmaz Karamdoust (2012)
10.1016/J.APSUSC.2006.10.054
Thiolated polyethylene oxide as a non-fouling element for nano-patterned bio-devices
Patricia Lisboa (2007)
10.7939/R3891249S
Human Plasma Adsorption to Biomaterials: Fundamental Level Chemical Modifications and Their Effects on Biocompatibility
Markian S Bahniuk (2017)
10.1007/978-3-319-45433-7
The Immune Response to Implanted Materials and Devices: The Impact of the Immune System on the Success of an Implant
B. Corradetti (2017)
10.1021/la3029935
Nonfouling poly(ethylene oxide) layers end-tethered to polydopamine.
O. Pop-Georgievski (2012)
10.1021/ACS.ANALCHEM.6B02617
Copolymer Brush-Based Ultralow-Fouling Biorecognition Surface Platform for Food Safety.
Hana Vaisocherová-Lísalová (2016)
10.1002/JBM.A.30977
Protein adsorption on polyurethane catheters modified with a novel antithrombin-heparin covalent complex.
Y. J. Du (2007)
10.1021/la4005483
Protein adsorption on well-characterized polyethylene oxide brushes on gold: dependence on molecular weight and grafting density.
W. Taylor (2013)
10.1016/J.SNB.2007.07.130
Surface passivation using oligo(ethylene glycol) in ATRP-assisted DNA detection
Xinhui Lou (2008)
10.1201/B11116-9
Polymer-Based Biocompatible Surface Coatings
Kai Yu (2011)
10.1615/JLONGTERMEFFMEDIMPLANTS.V21.I2.10
Short-term and long-term effects of orthopedic biodegradable implants.
A. Amini (2011)
10.1177/193229680800200628
Anti-Inflammatory Polymeric Coatings for Implantable Biomaterials and Devices
A. W. Bridges (2008)
10.1002/bit.24559
Engineering biomaterials to integrate and heal: The biocompatibility paradigm shifts
J. Bryers (2012)
10.1016/j.colsurfb.2016.01.064
Effect of hydrophilicity of end-grafted polymers on protein adsorption behavior: A Monte Carlo study.
Y. Han (2016)
10.1016/j.cbpa.2011.04.021
Protein interactions with surfaces: cellular responses, complement activation, and newer methods.
L. M. Szott (2011)
10.1016/J.MEMSCI.2012.02.061
Modification of ultrafiltration membranes with block copolymer nanolayers for produced water treatment: The roles of polymer chain density and polymerization time on performance
Daniel Wandera (2012)
Ionic strength and pH-dependent conformation of mixed polymer brushes for cycles of protein adsorption and desorption
M. Delcroix (2013)
10.1002/9781119655053.ch1
Anti‐Adhesive Coatings: A Technique for Prevention of Bacterial Surface Fouling
X. Sun (2020)
10.1002/POLA.24517
Multi‐functional initiator and poly(carboxybetaine methacrylamides) for building biocompatible surfaces using “nitroxide mediated free radical polymerization” strategies
Sinoj Abraham (2011)
10.1080/08927014.2014.897335
Amphiphilic triblock copolymers with PEGylated hydrocarbon structures as environmentally friendly marine antifouling and fouling-release coatings
Zhaoli Zhou (2014)
See more
Semantic Scholar Logo Some data provided by SemanticScholar