Temperature Dependence of the Protein Resistance of Poly- and Oligo(ethylene glycol)-Terminated Alkanethiolate Monolayers

Langmuir ◽  
2001 ◽  
Vol 17 (19) ◽  
pp. 5717-5720 ◽  
Author(s):  
Dirk Schwendel ◽  
Reiner Dahint ◽  
Sascha Herrwerth ◽  
Matthias Schloerholz ◽  
Wolfgang Eck ◽  
...  
Keyword(s):  
Ethylene Glycol ◽  
Temperature Dependence ◽  
Protein Resistance

scholarly journals Protein resistance of dextran and dextran-poly(ethylene glycol) copolymer films

Biofouling ◽  
2011 ◽  
Vol 27 (5) ◽  
pp. 497-503 ◽  
Author(s):  
Darby Kozak ◽  
Annie Chen ◽  
Jacinda Bax ◽  
Matt Trau
Keyword(s):  
Ethylene Glycol ◽  
Poly Ethylene Glycol ◽  
Protein Resistance ◽  
Copolymer Films ◽  
Poly Ethylene

Enhanced Power Factor of PEDOT:PSS Films Post-treated Using a Combination of Ethylene Glycol and Metal Chlorides and Temperature Dependence of Electronic Transport (325–450 K)

2020 ◽  
Vol 3 (12) ◽  
pp. 12447-12459
Author(s):  
Immanuel Paulraj ◽  
Tzu-Fang Liang ◽  
Tzyy-Schiuan Yang ◽  
Chia-Hsin Wang ◽  
Jeng-Lung Chen ◽  
...  
Keyword(s):  
Ethylene Glycol ◽  
Temperature Dependence ◽  
Power Factor ◽  
Electronic Transport ◽  
Metal Chlorides

Protein Resistance of Surfaces Modified with Oligo(Ethylene Glycol) Aryl Diazonium Derivatives

ChemPhysChem ◽  
2013 ◽  
Vol 14 (10) ◽  
pp. 2183-2189 ◽  
Author(s):  
Callie Fairman ◽  
Joshua Z. Ginges ◽  
Stuart B. Lowe ◽  
J. Justin Gooding
Keyword(s):  
Ethylene Glycol ◽  
Protein Resistance

Positronium Lifetime Study on Subnanoscopic Structure of Polyrotaxane

2012 ◽  
Vol 733 ◽  
pp. 167-170
Author(s):  
K. Ito ◽  
Chang Ming Zhao ◽  
Kohzo Ito ◽  
Yoshinori Kobayashi
Keyword(s):  
Ethylene Glycol ◽  
Temperature Dependence ◽  
Positron Annihilation ◽  
Chemical Structure ◽  
Poly Ethylene Glycol ◽  
Positron Annihilation Lifetime ◽  
Positronium Lifetime ◽  
End Groups ◽  
Poly Ethylene ◽  
Free Volume Hole

The subnanoscopic structures of polyrotaxanes, prepared from α-cyclodextrins, poly(ethylene glycol), and bulky adamantane end groups, were examined by means of the positron annihilation lifetime technique, in consideration of the free-volume hole, quantified from the long-lived ortho-positronium (o-Ps) lifetimes. The influence of the chemical structure on the temperature dependence of the o-Ps lifetimes are discussed.

Formation, Characterization, Protein Resistance, and Reactivity of Cl3Si(CH2)11(OCH2CH2)3OH Self-Assembled Monolayers

2002 ◽  
Vol 724 ◽  
Author(s):  
Jiehyun Seong ◽  
Seok-Won Lee ◽  
Paul E. Laibinis
Keyword(s):  
Ethylene Glycol ◽  
Chemical Modification ◽  
Self Assembly ◽  
Protein A ◽  
Self Assembled Monolayers ◽  
Protecting Group ◽  
Protein Resistance ◽  
Attachment Sites ◽  
Assembled Monolayers ◽  
Selective Immobilization

AbstractWe report a method for generating tri(ethylene glycol)-terminated-n-alkyltrichlorosiloxane monolayers on SiO2 surfaces. These chemisorbed films, with a thickess of ∼2-3 nm, provide an oligo(ethylene glycol) surface that reduces the nonspecific adsorption of proteins and hydroxyl attachment sites for covalently immobilizing biomolecules to the substrate. These mono-molecular films were formed by adsorbing an acetoxy-tri(ethylene glycol)-terminated n-alkyltrichlorosilane, CH3(C=O)O(CH2CH2O)3(CH2)11SiCl3, onto glass and Si/SiO2 substrates, where the terminal acetate provided a protecting group for the hydroxyl functionality during self-assembly of the film. After formation of the monolayer, the acetate functionality was reduced chemically to form films exposing a covalently attached -(OCH2CH2)3OH terminus at a density of ∼3[.dotmath]1014 molecules/cm2. Protein adsorption studies verified that the films exhibited notable resistances against the non-specific adsorption of various proteins. Chemical modification of the -(OCH2CH2)3OH surface with protein A provided a non-adsorbing surface for selective immobilization of immunoglobulins.

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