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Papers In Press, published online ahead of print April 30, 2003
Department of Pathology and Laboratory Medicine, University of Cincinnati, Cincinnati, OH 45267-0529
Corresponding Author: Sean.Davidson{at}UC.edu
The three-dimensional structure of human apoA-I on nascent, discoidal HDL particles has been debated extensively over the past 25 years. Recent evidence has demonstrated that the a-helical domains of apoA-I are arranged in a belt-like orientation with the long axis of the helices perpendicular to the phospholipid acyl chains on the disc edge. However, experimental information on the spatial relationships between apoA-I molecules on the disc is lacking. To address this issue, we have taken advantage of recent advances in mass spectrometry technology combined with cleavable cross-linking chemistry to derive a set of distance constraints suitable for testing apoA-I structural models. We generated highly homogeneous, reconstituted HDL (rHDL) particles containing two molecules of apoA-I. These were treated with a thiol-cleavable cross-linking agent, which covalently joined Lys residues in close proximity within or between molecules of apoA-I in the disc. The cross-linked discs were then exhaustively trypsinized to generate a discrete population of peptides. The resulting peptides were analyzed by liquid chromatography / mass spectrometry before and after cleavage of the cross-links and resulting peaks were identified based on the theoretical tryptic cleavage of apoA-I. The results indicated that at least 19 of the 21 Lys residues within apoA-I were modifiable by the cross-linker. We identified at least 8 intramolecular and 7 intermolecular cross-links in the particle. The distance constraints are used to analyze three current models of apoA-I structure. The results strongly support the presence of the salt-bridge interactions that were predicted to occur in the “double belt” model of apoA-I, but a helical hairpin model containing the same salt-bridge docking interface is also consistent with the data.
J. Biol. Chem, 10.1074/jbc.M302764200
Submitted on March 18, 2003
Revised on April 28, 2003
Accepted on April 30, 2003
The spatial organization of apolipoprotein A-I on the edge of discoidal high-density lipoprotein particles: A mass spectrometry study
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