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20231223080521.0 |
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231223s2005 xx ||||| 00| ||eng c |
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|a pubmed24n0525.xml
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|a (DE-627)NLM157597164
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|a (NLM)16142960
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|a DE-627
|b ger
|c DE-627
|e rakwb
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| 041 |
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|a eng
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| 100 |
1 |
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|a Lazos, Dimitrios
|e verfasserin
|4 aut
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| 245 |
1 |
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|a Size-selective protein adsorption to polystyrene surfaces by self-assembled grafted poly(ethylene glycols) with varied chain lengths
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|c 2005
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|a Text
|b txt
|2 rdacontent
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|a ohne Hilfsmittel zu benutzen
|b n
|2 rdamedia
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|a Band
|b nc
|2 rdacarrier
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|a Date Completed 28.03.2007
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|a Date Revised 10.03.2022
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|a published: Print
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|a Citation Status MEDLINE
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|a We report about the surface modification of polystyrene (PSt) with photoreactive alpha-4-azidobenzoyl-omega-methoxy poly(ethylene glycol)s (ABMPEG) of three different molecular weights (MWs of approximately 2, approximately 5, and approximately 10 kg/mol) and with two poly(ethylene glycol)/poly(propylene glycol) triblock copolymers (PEG-PPG-PEG) of about identical PEG/PPG ratio (80/20, w/w) and MW(PEG) of approximately 3 and approximately 6 kg/mol, all via adsorption from aqueous solutions. For ABMPEGs, an additional UV irradiation was used for photografting to the PSt. Contact angle (CA) and atomic force microscopy data revealed pronounced differences of the hydrophilicity/hydrophobicity and topography of the surfaces as a function of PEG type and concentration used for the modification. In all cases, an incomplete coverage of the PSt was observed even after modification at the highest solution concentrations (10 g/L). However, clear differences were seen between PEG-PPG-PEGs and ABMPEGs; only for the latter was a nanoscale-ordered interphase structure with an influence of MW(PEG) on the PEG density observed; after modification at the same solution concentrations, the density was significantly higher for lower MW(PEG). The adsorption of three proteins, myoglobin (Mgb), bovine serum albumin (BSA), and fibrinogen to the various surfaces was analyzed by surface plasmon resonance. Pronounced differences between the two PEG types with respect to the reduction of protein adsorption were found. At high, but still incomplete, surface coverage and similar CA, the shielding of ABMPEG layers toward the adsorption of Mgb and BSA was much more efficient; e.g., the adsorbed Mgb mass relative to that of unmodified PSt was reduced to 10% for ABMPEG 2 kg/mol while for both PEG-PPG-PEGs the Mgb mass was still around 100%. In addition, for the ABMPEG layers an effect of MW(PEG) on adsorbed protein mass-decrease with decreasing MW-could be confirmed; and the highest Mgb/BSA selectivities were also observed. A "two-dimensional molecular sieving", based on PEG molecules having a nanoscale order at the hydrophobic substrate polymer surface has been proposed, and the main prerequisites were the use of PEG conjugates which are suitable for an "end-on" grafting (e.g., ABMPEGs), the use of suitable (not too high) concentrations for the surface modification via adsorption/self-assembly, optionally the photografting on the substrate (possible only for ABMPEG), and presumably, a washing step to remove the excess of unbound PEGs. The results of this study also strongly support the hypothesis that the biocompatibility of hydrophobic materials can be very much improved by PEG modifications at surface coverages that are incomplete but have an ordered layer structure controlled by the size and steric interactions of surface-bound PEGs
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|a Journal Article
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|a Myoglobin
|2 NLM
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|a Polystyrenes
|2 NLM
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|a Solutions
|2 NLM
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|a Water
|2 NLM
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|a 059QF0KO0R
|2 NLM
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|a Serum Albumin, Bovine
|2 NLM
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| 650 |
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|a 27432CM55Q
|2 NLM
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| 650 |
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7 |
|a Polyethylene Glycols
|2 NLM
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| 650 |
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|a 3WJQ0SDW1A
|2 NLM
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|a Fibrinogen
|2 NLM
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| 650 |
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|a 9001-32-5
|2 NLM
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| 700 |
1 |
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|a Franzka, Steffen
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Ulbricht, Mathias
|e verfasserin
|4 aut
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| 773 |
0 |
8 |
|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 21(2005), 19 vom: 13. Sept., Seite 8774-84
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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| 773 |
1 |
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|g volume:21
|g year:2005
|g number:19
|g day:13
|g month:09
|g pages:8774-84
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|a GBV_USEFLAG_A
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|a SYSFLAG_A
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|a GBV_NLM
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|a GBV_ILN_22
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|a GBV_ILN_350
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|a GBV_ILN_721
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|a AR
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| 952 |
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|d 21
|j 2005
|e 19
|b 13
|c 09
|h 8774-84
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