Chemical Engineering / Kimya Mühendisliği
Permanent URI for this collectionhttps://hdl.handle.net/11147/14
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Article Citation - WoS: 24Citation - Scopus: 24Synthesis of Heterotelechelic Polymers With Affinity To Glutathione-S and Biotin-Tagged Proteins by Raft Polymerization and Thiol-Ene Reactions(Royal Society of Chemistry, 2011) Huang, Xin; Boyer, Cyrille; Davis, Thomas P.; Bulmuş, Volgaα-Glutathione (GSH), ω-biotin functionalized poly(N-isopropylacrylamide) (PNIPAAm) was synthesized via reversible addition-fragmentation chain transfer (RAFT) polymerization using a new R-group allyl functionalized trithiocarbonate chain transfer agent (CTA) and thiol-ene reactions. GPC and 1H NMR results indicated that the allyl group had no adverse effect on the RAFT-controlled polymerization of NIPAAm and PEG-A, and the new CTA could efficiently control the polymerizations. Employing radical thiol-ene and Michael addition reactions, heterotelechelic α-allyl, ω-carboxylic acid-PNIPAAm was first aminolyzed in the presence of maleimide-modified biotin and subsequently reacted with GSH via radical thiol-ene addition to yield α-GSH, ω-biotin functionalized PNIPAAm. Glutathione S-transferase (GST) and streptavidin (SAv) were coupled in solution with heterofunctional PNIPAAm via bioaffinity interactions. Separately, α-GSH, ω-biotin functionalized PNIPAAm was further shown to bind GST-tagged Rac1, a potential cancer marker, and biotin-tagged bovine serum albumin (BSA).