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. 1974 Sep;71(9):3696–3700. doi: 10.1073/pnas.71.9.3696

13C Nuclear Magnetic Resonance Spectroscopic Evidence for Hydrophobic Lipid-Protein Interactions in Human High Density Lipoproteins

Wilhelm Stoffel 1, Ottfried Zierenberg 1, Budi Tunggal 1, Ekkehard Schreiber 1
PMCID: PMC433843  PMID: 4372633

Abstract

Phosphatidylcholines, sphingomyelins, cholesterol, and cholesterol esters were enriched with 13C by chemical synthesis in specific positions of their hydrophilic groups and aliphatic chains. Their spin-lattice relaxation times were determined in organic solvents. The substances were organized as liposomes and recombined with total human high density apolipoproteins and the two separated main components, apolipoprotein A-I (apoLp-Gln-I) and apolipoprotein A-II (apoLp-Gln-II).

These 13C nuclear magnetic resonance data established that in reassembled high density lipoproteins the phospholipid molecules bind to the apoprotein moieties with their hydrophobic fatty acid chains and not with their hydrophilic zwitterionic groups. Apolipoprotein A-I preferentially binds phosphatidylcholine, although its lipid-binding capacity is smaller than that of apolipoprotein A-II. Apolipoprotein A-II avidly reassembles with sphingomyelin by hydrophobic interactions. A model of the molecular organization of the high density lipoportein particle has been derived.

Keywords: reassembling of [13C]lipids and high density apolipoproteins, spin lattice relaxation

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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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