Improved properties of the non-covalent coating with N,N-didodecyl-N, N-dimethylammonium bromide for the separation of basic proteins by capillary electrophoresis with acidic buffers in 25 ?m capillaries
Improved properties of the non-covalent coating with N,N-didodecyl-N, N-dimethylammonium bromide for the separation of basic proteins by capillary electrophoresis with acidic buffers in 25 ?m capillaries
Engineering Village 2
? 2006 Elsevier Inc
Accession number: 06249936656
Title: Interconverting conformations of variants of the human amyloidogenic protein ?2-microglobulin quantitatively characterized by dynamic capillary electrophoresis and computer simulation
Authors: Heegaard, Niels H. H.; Jorgensen, Thomas J. D.; Cheng, Lei; Schou, Christian; Nissen, Mogens H.; Trapp, Oliver
Author affiliation: Statens Serum Institut, Copenhagen, Denmark
Serial title: Analytical Chemistry
Abbreviated serial title: Anal. Chem.
Volume: v 78
Issue: n 11
Issue date: Jun 1 2006
Publication year: 2006
Pages: p 3667-3673
Language: English
ISSN: 0003-2700
CODEN: ANCHAM
Document type: Journal article (JA)
Publisher: American Chemical Society, Columbus, OH 43210-3337, United States
Abstract: Capillary electrophoretic separation profiles of cleaved variants of ?2-microglobulin (?2m) reflect the conformational equilibria existing in solutions of these proteins. The characterization of these equilibria is of interest since ?2m is responsible for amyloid formation in dialysis-related amyloidosis and thus is able to attain alternative conformations that lead to irreversible aggregation and precipitation. In this study, we quantitate the increased conformational instability of cleaved ?2m by extracting rate constants and activation energies by simulating the experimental data using a unified theory for dynamic chromatography and dynamic electrophoresis. The results are correlated with the outcome of independent experiments based on mass spectrometric measurement of H/D exchange. This study illustrates that dynamic capillary electrophoresis is suitable for the investigation of the interconversion of protein conformations of amyloidogenic molecules and is not only restricted to ideal model compounds. ? 2006 American Chemical Society.
Number of references: 35
Ei main heading: Proteins
Ei controlled terms: Electrophoresis - Computer simulation - Precipitation (chemical) - Agglomeration - Chromatographic analysis - Mass spectrometry
Uncontrolled terms: Amyloidogenic protein - Microglobulin - Dynamic capillary electrophoresis - Irreversible aggregation
Ei classification codes: 804.1 Organic Compounds - 801.4.1 Electrochemistry - 802.3 Chemical Operations
Treatment: Theoretical (THR); Experimental (EXP)
DOI: 10.1021/ac060194m
Database: Compendex
Compilation and indexing terms, ? 2006 Elsevier Inc. All rights reserved
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