Congophilicity (Congo red affinity) of different beta2-microglobulin conformations characterized by dye affinity capillary electrophoresis.
Research output: Contribution to journal › Journal article › peer-review
The amyloidogenic protein beta-microglobulin was characterized by affinity capillary electrophoresis (CE). CE could separate conformational variants of beta2-microglobulin and with the amyloid-specific dye Congo red as a buffer additive it was possible to measure different Congo red-affinities of native and abnormally folded beta2-microglobulin. We find that native beta2-microglobulin has an intermediate affinity for Congo red at pH 7.3 and that binding involves electrostatic interactions. The conformational variant of beta2-microglobulin that appears in acetonitrile solutions binds Congo red more strongly. Affinity CE using Congo red as a buffer additive is a new, simple, fast, and quantitative micromethod for the characterization of soluble conformational intermediates of amyloidogenic proteins.
Original language | English |
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Journal | Journal of Chromatography A |
Volume | 894 |
Issue number | 1-2 |
Pages (from-to) | 319-27 |
Number of pages | 8 |
ISSN | 0021-9673 |
Publication status | Published - 2000 |
Bibliographical note
Keywords: Coloring Agents; Congo Red; Electrophoresis, Capillary; Mass Spectrometry; Protein Conformation; beta 2-Microglobulin
ID: 8746353