Nanoengineered analytical immobilized metal affinity chromatography stationary phase by atom transfer radical polymerization: separation of synthetic prion peptides.

Nanoengineered analytical immobilized metal affinity chromatography stationary phase by atom transfer radical polymerization: separation of synthetic prion peptides. Research Abstract Details 

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Nanoengineered analytical immobilized metal affinity chromatography stationary phase by atom transfer radical polymerization: separation of synthetic prion peptides. Abstract Text:

P McCarthy,M Chattopadhyay,G L Millhauser,N V Tsarevsky,L Bombalski,K Matyjaszewski,D Shimmin,N Avdalovic,C Pohl,

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.

Nanoengineered analytical immobilized metal affinity chromatography stationary phase by atom transfer radical polymerization: separation of synthetic prion peptides. Publishing Authors By Initials

P McCarthy,M Chattopadhyay,GL Millhauser,NV Tsarevsky,L Bombalski,K Matyjaszewski,D Shimmin,N Avdalovic,C Pohl,

For similar proteins: prions research abstracts see: proteins: prions research

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Nanoengineered analytical immobilized metal affinity chromatography stationary phase by atom transfer radical polymerization: separation of synthetic prion peptides. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Analytical biochemistry

VOLUME: 366

Page Numbers: 1-8

Journal Abbreviation: Anal. Biochem.

ISSN: 0003-2697

DAY: 13

MONTH: 03

YEAR: 2007

Nanoengineered analytical immobilized metal affinity chromatography stationary phase by atom transfer radical polymerization: separation of synthetic prion peptides. Information

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LANGUAGE: eng

NlmUniqueID: 370535

Nanoengineered analytical immobilized metal affinity chromatography stationary phase by atom transfer radical polymerization: separation of synthetic prion peptides. Keywords Mesh Terms:

KEYWORDS: Prions

MESH TERMS: isolation & purification

Chemical & Substance for Abstract: Nanoengineered analytical immobilized metal affinity chromatography stationary phase by atom transfer radical polymerization: separation of synthetic prion peptides. Information

Substance Name: Prions

Registry Number: 0

Grant and Affiliation Information for Nanoengineered analytical immobilized metal affinity chromatography stationary phase by atom transfer radical polymerization: separation of synthetic prion peptides.

AFFILIATION: Research and Development, Dionex Corporation, Sunnyvale, CA 94088, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: GM 65790

ACRONYM: GM

MEDLINETA: Anal Biochem

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