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Two Apolipoprotein E Mimetic Peptides, ApoE(130−149) and ApoE(141−155)2, Bind to LRP1

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    Two Apolipoprotein E Mimetic Peptides, ApoE(130−149) and ApoE(141−155)2, Bind to LRP1†
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    Department of Chemistry and Biochemistry, University of California at San Diego, 9500 Gilman Drive, La Jolla, California 92093-0378
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    Biochemistry

    Cite this: Biochemistry 2004, 43, 23, 7328–7335
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    https://doi.org/10.1021/bi036208p
    Published May 20, 2004
    Copyright © 2004 American Chemical Society
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    Abstract

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    LRP1 is a cell surface receptor responsible for clearing some 30 known ligands. We have previously shown that each of the three complete LDL receptor-homology domains of the LRP1 extracellular domain (sLRPs) binds apoE-enriched β-VLDL particles. Here we show that two peptides from the N-terminal receptor binding domain of apoE, which are known to elicit a number of different cellular responses, bind to LRP1. Solution binding assays show that the two peptides, apoE(130−149) and apoE(141−155)2, interact with each of the sLRPs (2, 3, and 4). Each peptide was found to exhibit the same solution binding characteristics as apoE-enriched β-VLDL particles. Surface plasmon resonance analyses of the sLRP−apoE peptide interaction show that both peptides bind the sLRPs with KD values in the 100 nM range, a value similar to the effective concentration required for observation of the cellular responses. Consistent with results from mutagenesis studies of binding of apoE to LDLR, apoE(130−149,Arg142Glu) bound with a KD similar to that of the wild-type sequence, while apoE(130−149,Lys143Glu) showed a 10-fold decrease in KD. Each of the peptides bound heparin, and heparin competed for sLRP binding.

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    †

     This work was supported by NIH Grant AG17992.

    *

     To whom correspondence should be addressed. Phone:  (858) 534-3058. Fax:  (858) 534-6174. E-mail:  [email protected].

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    Biochemistry

    Cite this: Biochemistry 2004, 43, 23, 7328–7335
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    https://doi.org/10.1021/bi036208p
    Published May 20, 2004
    Copyright © 2004 American Chemical Society
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