Corpus ID: 28439604

Structural features of synthetic peptides of apolipoprotein E that bind the LDL receptor.

@article{Dyer1995StructuralFO,
  title={Structural features of synthetic peptides of apolipoprotein E that bind the LDL receptor.},
  author={C. Dyer and D. Cistola and G. Parry and L. Curtiss},
  journal={Journal of lipid research},
  year={1995},
  volume={36 1},
  pages={
          80-8
        }
}
  • C. Dyer, D. Cistola, +1 author L. Curtiss
  • Published 1995
  • Chemistry, Medicine
  • Journal of lipid research
  • Apolipoprotein (apo) E, via its receptor binding domain contained in residues 140-150, mediates hepatic and peripheral tissue binding of cholesterol-rich lipoproteins. Previously, we reported that a synthetic peptide representing a linear tandem repeat of amino acids 141-155, the 141-155 dimer, binds the low density lipoprotein (LDL) receptor. To define the structural features essential for LDL receptor binding of the 141-155 dimer, a series of modified peptides were synthesized. The secondary… CONTINUE READING
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