NR AXFQ
AU McCarthy,P.; Chattopadhyay,M.; Millhauser,G.L.; Tsarevsky,N.V.; Bombalski,L.; Matyjaszewski,K.; Shimmin,D.; Avdalovic,N.; Pohl,C.
TI Nanoengineered analytical immobilized metal affinity chromatography stationary phase by atom transfer radical polymerization: separation of synthetic prion peptides.
QU Analytical Biochemistry 2007 Jul 1; 366(1): 1-8
PT journal article; research support, n.i.h., extramural; research support, u.s. gov't, non-p.h.s.
AB Atom transfer radical polymerization (ATRP) was employed to create isolated, metal-containing nanoparticles on the surface of nonporous polymeric beads with the goal of developing a new immobilized metal affinity chromatography (IMAC) stationary phase for separating prion peptides and proteins. Transmission electron microscopy was used to visualize nanoparticles on the substrate surface. Individual ferritin molecules were also visualized as ferritin-nanoparticle complexes. The column's resolving power was tested by synthesizing peptide analogs to the copper binding region of prion protein and injecting mixtures of these analogs onto the column. As expected, the column was capable of separating prion-related peptides differing in number of octapeptide repeat units (PHGGGWGQ), (PHGGGWGQ)(2), and (PHGGGWGQ)(4). Unexpectedly, the column could also resolve peptides containing the same number of repeats but differing only in the presence of a hydrophilic tail, Q-->A substitution, or amide nitrogen methylation.
MH Amino Acid Sequence; Animals; Chromatography, Affinity/*methods; Humans; Metals; Nanotechnology; Peptide Fragments/chemical synthesis/chemistry/isolation & purification; Prions/chemical synthesis/chemistry/*isolation & purification
AD Research and Development, Dionex Corporation, Sunnyvale, CA 94088, USA.
SP englisch
PO USA