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|Title:||Synthesis of heterotelechelic polymers with affinity to glutathione-S-transferase and biotin-tagged proteins by RAFT polymerization and thiol-ene reactions||Authors:||Huang, Xin
Davis, Thomas P.
Bovine serum albumins
Chain transfer agents
|Issue Date:||Jul-2011||Publisher:||Royal Society of Chemistry||Source:||Huang, X., Boyer, C., Davis, T. P., and Bulmus, V. (2011). Synthesis of heterotelechelic polymers with affinity to glutathione-S-transferase and biotin-tagged proteins by RAFT polymerization and thiol-ene reactions. Polymer Chemistry, 2(7), 1505-1512. doi:10.1039/c1py00049g||Abstract:||α-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).||URI:||https://doi.org/10.1039/c1py00049g
|Appears in Collections:||Chemical Engineering / Kimya Mühendisliği|
Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection
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