PMID: 11904224Mar 21, 2002Paper

Folding and stability of the C-terminal half of apolipoprotein A-I examined with a Cys-specific fluorescence probe

Biochimica Et Biophysica Acta
A K Behling AgreeA Jonas

Abstract

Apolipoprotein A-I (apoA-I) has important physiologic roles in reverse cholesterol transport, as a component of HDL; however, apoA-I also exists in lipid-poor or lipid-free forms that are key intermediates in HDL metabolism and acceptors of lipids from cells. The aim of this study was to examine the structure and stability of the central and C-terminal regions of lipid-free apoA-I. To this end, five Cys mutants of proapoA-I were constructed and expressed in Escherichia coli: V119C, A124C, A154C, A190C, and A232C. These mutants were specifically labeled with 6-acryloyl-2-dimethylaminonaphthalene (acrylodan, AC) and were examined by CD spectroscopy and a variety of fluorescence methods. The results showed that the introduction of Cys residues and their covalent labeling with AC did not affect the overall structure and stability of apoA-I. However, AC fluorescence properties revealed that different segments of the central and C-terminal half of apoA-I have distinct folding and stability properties. From fluorescence energy transfer data, average distances between the N-terminal region containing Trp residues and the various AC locations were obtained. The current results, together with previously published observations, led to the...Continue Reading

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Citations

Sep 19, 2012·The Protein Journal·Eduardo Daniel PrietoHoracio Alberto Garda
Nov 5, 2010·The Journal of Biological Chemistry·Jens O LagerstedtMichael N Oda
May 12, 2004·Analytical Biochemistry·Andrey S KlymchenkoAlexander P Demchenko
Feb 24, 2006·Biochimica Et Biophysica Acta·Gregory BrubakerJonathan D Smith
Sep 28, 2010·Journal of Molecular Graphics & Modelling·Alessandro Guerini RoccoIvano Eberini
Aug 11, 2005·The Journal of Biological Chemistry·Dao-Quan PengJonathan D Smith

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