Poly(l-lysine)-g-Poly(ethylene glycol) Layers on Metal Oxide Surfaces:  Attachment Mechanism and Effects of Polymer Architecture on Resistance to Protein Adsorption†

2000 ◽  
Vol 104 (14) ◽  
pp. 3298-3309 ◽  
Author(s):  
Gregory L. Kenausis ◽  
Janos Vörös ◽  
Donald L. Elbert ◽  
Ningping Huang ◽  
Rolf Hofer ◽  
...  
Biochemistry ◽  
2000 ◽  
Vol 39 (12) ◽  
pp. 3441-3451 ◽  
Author(s):  
Nadezhda V. Efremova ◽  
Bruce Bondurant ◽  
David F. O'Brie ◽  
Deborah E. Leckband

2013 ◽  
Vol 13 (12) ◽  
pp. 1720-1729 ◽  
Author(s):  
Axel T. Neffe ◽  
Maik von Ruesten-Lange ◽  
Steffen Braune ◽  
Karola Luetzow ◽  
Toralf Roch ◽  
...  

2019 ◽  
Vol 10 (31) ◽  
pp. 7333-7339 ◽  
Author(s):  
Zhao Zheng ◽  
Qianjie Zhou ◽  
Mu Li ◽  
Panchao Yin

PEG–POM nanocomposites are ideal candidates for semi-solid proton conductors with high proton conductivities and devisable mechanical performances.


2005 ◽  
Vol 58 (4) ◽  
pp. 275 ◽  
Author(s):  
Alison J. Downard ◽  
Sandra L. Jackson ◽  
Emelyn S. Q. Tan

Glassy carbon (GC) surfaces were modified with thin films by means of electrochemically assisted reduction of aryl diazonium salts and oxidation of primary amines. GC plates with modified and unmodified areas were exposed to solutions of fluorescently labelled bovine serum albumin (BSA-FITC). Fluorescence microscopy was found to be a simple and direct method for comparing adsorption of BSA-FITC between the different areas. Modification with methylbenzene, hexylbenzene, poly(ethylene glycol) benzene, and tetraethylene glycol diamine groups increases protein adsorption relative to unmodified GC. Hexylamine and the poly(ethylene glycol) diamine ED-2003 reduce protein adsorption. The results give insight into some factors controlling protein adsorption at these surface films.


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