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={Cheryl A. Dyer and David P Cistola and Graham C Parry and Linda K. Curtiss},
  journal={Journal of lipid research},
  year={1995},
  volume={36 1},
  pages={
          80-8
        }
}
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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