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. 1974 Mar;71(3):989–993. doi: 10.1073/pnas.71.3.989

Lipid-Protein Interactions in High Density Lipoproteins

Gerd Assmann 1, H Bryan Brewer Jr 1
PMCID: PMC388143  PMID: 4362643

Abstract

Delipidated high density lipoprotein (apo-HDL), isolated apolipoproteins apoA-I and apoA-II, S-carboxymethylated apoA-II, apoC-III, the NH2- and COOH-terminal CNBr peptides of apoA-II, and the COOH-terminal CNBr peptide of apoA-I were recombined in vitro with [N-C3H3-choline]phosphatidylcholine (PC) and [N-14CH3-choline]sphingomyelin (SPM). The lipid-protein complexes were analyzed by ultracentrifugal flotation, agarose gel chromatography and circular dichroism. ApoHDL, apoA-II, and S-carboxymethylated apoA-II readily recombined with PC or SPM to form particles that were similar in size to native HDL. The COOH- but not the NH2-terminal CNBr peptide of apoA-II recombined with lipid. ApoA-I and the COOH-terminal CNBr peptide of apoA-I, however, recombined with PC or SPM to only a limited extent, suggesting that protein-protein interactions between apoA-I and apoA-II are important in the integration of apoA-I into recombined lipoprotein particles. Analysis of the recombined lipid-protein complexes by circular dichroism indicated that there was an increase in helical structure concomitant with lipid-protein binding. The reconstituted particles had many of the physical and chemical properties of the native lipoprotein.

Keywords: recombination of apolipoproteins with phospholipids, circular dichroism and gel chromatography of recombined lipid-protein particles

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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