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231224s2013 xx |||||o 00| ||eng c |
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|a 10.1021/la400721c
|2 doi
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|a pubmed24n0761.xml
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|a (DE-627)NLM228547237
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|a (NLM)23790067
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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|a Flavel, Benjamin S
|e verfasserin
|4 aut
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|a Grafting of poly(ethylene glycol) on click chemistry modified Si(100) surfaces
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|c 2013
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
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|2 rdamedia
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|a ƒa Online-Ressource
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|2 rdacarrier
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|a Date Completed 22.01.2014
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|a Date Revised 03.12.2018
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Poly(ethylene glycol) (PEG) is one of the most extensively studied antifouling coatings due to its ability to reduce protein adsorption and improve biocompatibility. Although the use of PEG for antifouling coatings is well established, the stability and density of PEG layers are often inadequate to provide optimum antifouling properties. To improve on these shortcomings, we employed the stepwise construction of PEG layers onto a silicon surface. Acetylene-terminated alkyl monolayers were attached to nonoxidized crystalline silicon surfaces via a one-step hydrosilylation procedure with 1,8-nonadiyne. The acetylene-terminated surfaces were functionalized via a copper-catalyzed azide-alkyne cycloaddition (CuAAC) reaction of the surface-bound alkynes with an azide to produce an amine terminated layer. The amine terminated layer was then further conjugated with PEG to produce an antifouling surface. The antifouling surface properties were investigated by testing adsorption of human serum albumin (HSA) and lysozyme (Lys) onto PEG layers from phosphate buffer solutions. Detailed characterization of protein fouling was carried out with X-ray photoelectron spectroscopy (XPS) and time-of-flight secondary ion mass spectrometry (ToF-SIMS) combined with principal component analysis (PCA). The results revealed no fouling of albumin onto PEG coatings whereas the smaller protein lysozyme adsorbed to a very low extent
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|a Journal Article
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|a Alkynes
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|a Azides
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|a Serum Albumin, Bovine
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|a 27432CM55Q
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|a Polyethylene Glycols
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|a 3WJQ0SDW1A
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|a Muramidase
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|a EC 3.2.1.17
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|a Silicon
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|a Z4152N8IUI
|2 NLM
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|a Jasieniak, Marek
|e verfasserin
|4 aut
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|a Velleman, Leonora
|e verfasserin
|4 aut
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|a Ciampi, Simone
|e verfasserin
|4 aut
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|a Luais, Erwann
|e verfasserin
|4 aut
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|a Peterson, Joshua R
|e verfasserin
|4 aut
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|a Griesser, Hans J
|e verfasserin
|4 aut
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|a Shapter, Joe G
|e verfasserin
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|a Gooding, J Justin
|e verfasserin
|4 aut
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 29(2013), 26 vom: 02. Juli, Seite 8355-62
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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| 773 |
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|g volume:29
|g year:2013
|g number:26
|g day:02
|g month:07
|g pages:8355-62
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|u http://dx.doi.org/10.1021/la400721c
|3 Volltext
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