@article {894,
	title = {Plasma protein adsorption to surfaces grafted with dense homopolymer and copolymer brushes containing poly(N-isopropylacrylamide)},
	journal = {Journal of Biomaterials Science-Polymer Edition},
	volume = {15},
	number = {9},
	year = {2004},
	note = {ISI Document Delivery No.: 865ALTimes Cited: 13Cited Reference Count: 38Symposium on Gels, Genes, Grafts and Giants held in Celebration of the 70th Birthday of Allan HoffmanDEC, 2002Maui, HIUniv Washington Engineered Biomat NSF Engn Res Ctr},
	pages = {1121-1135},
	type = {Proceedings Paper},
	abstract = {Growing polymer chains from surface initiators in principle allows much more dense polymer surface layers to be created than can be produced by grafting of whole (self-excluding) chains. We have utilized aqueous atom transfer radical polymerization to graft a series of cleavable hydrophilic poly (N-isopropylacrylamide) (PNIPAM) homopolymers and block copolymers of substituted acry-lamides from polystyrene latex to give brushes of controlled MW and surface density. Average chain separations much less than their free solution radii of gyration have been achieved. Exposure to radiolabeled single proteins or to whole plasma and subsequent analysis by SDS-PAGE shows that PNIPAM brushes decrease protein adsorption relative to the latex surface or other substituted polyacrylamides. The PNIPAM brushes exhibit a second-order phase transition around 30degreesC as reflected by a decrease in the hydrodynamic thickness of the brush at higher temperatures. Total plasma protein adsorption is increased at 40degreesC compared to 20degreesC but there is significant differential adsorption behavior among the proteins detected by gel-electrophoresis analysis.},
	keywords = {ADSORPTION, BIOMATERIALS, block copolymer, CHROMATOGRAPHY, FIBRINOGEN ADSORPTION, grafted latex, I-125 radiolabel, MODEL, OXIDE), plasma protein, POLY(ETHYLENE GLYCOL), POLY(N-ISOPROPYLACRYLAMIDE), polymer brush, POLYMER BRUSHES, PREVENTION, SDS-PAGE, SELF-ASSEMBLED MONOLAYERS, SERUM-ALBUMIN ADSORPTION},
	isbn = {0920-5063},
	url = {<Go to ISI>://000224674600005},
	author = {Janzen, J. and Le, Y. and Kizhakkedathu, J. N. and Brooks, D. E.}
}
@article {4210,
	title = {Inhibition of liposome-induced complement activation by incorporated poly(ethylene glycol) lipids},
	journal = {Archives of Biochemistry and Biophysics},
	volume = {357},
	number = {2},
	year = {1998},
	note = {ISI Document Delivery No.: 119UCTimes Cited: 65Cited Reference Count: 50},
	month = {Sep},
	pages = {185-194},
	type = {Article},
	abstract = {Complement activation causes opsonization of foreign particles leading to particle elimination from the blood. Complement-mediated opsonization of charged and large liposomes presents a fundamental problem in their use to deliver therapeutic agents in vivo. To prolong the circulation half-lives of such liposomes, complement activation must be curtailed. The aim of this study was to assess the ability of poly(ethylene glycol)-lipids (PEG-lipids) to inhibit the in vitro activation of the classical pathway of complement in human serum by anionic liposomes. Incorporation of cholesterol-PEG(600) (CH-PEG(600)), cholesterol-PEG(1000) (CH-PEG(1000)), or phosphatidylethanolamine-PEG(2000) (PE-PEG(2000)) resulted in dose-dependent inhibition of Clq binding and complement activation. The dose of PEG-lipid at which complement activation was blocked was inversely related to the PEG chain length. Complement activation was strongly inhibited when 15 mole\% of CH-PEG(600), 10 mole\% CH-PEG(1000), or 5 mole\% PE-PEG(2000), was incorporated into 100-nm anionic liposomes. PEG-lipid incorporation into larger liposomes (240 nm) was also successful in blocking C1q binding and complement activation. Radiolabeled cholesterol-PEG(similar to 1400) was prepared and used to determine both the percentage of CH-PEG incorporated into the liposomes and the percentage maintained in the liposomes in the presence of 50\% human serum at 37 degrees C for up to 24 h. (C) 1998 Academic Press.},
	keywords = {C1q, CHOLESTEROL, CLEARANCE, complement activation, HEPATIC-UPTAKE, INVIVO, LARGE UNILAMELLAR VESICLES, LIPOSOMES, POLY(ETHYLENE GLYCOL), POLYETHYLENE-GLYCOL, PROLONGED CIRCULATION TIME, SERUM, SIZE, SURFACE-CHARGE},
	isbn = {0003-9861},
	url = {<Go to ISI>://000075915200002},
	author = {Bradley, A. J. and Devine, D. V. and Ansell, S. M. and Janzen, J. and Brooks, D. E.}
}
