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Apolipoprotein E Mimetic Peptides: Cholesterol-Dependent and Cholesterol-Independent Properties

  • Chapter
Apolipoprotein Mimetics in the Management of Human Disease

Abstract

Apolipoprotein E (apoE) has a dual-domain structure, with a four-helix bundle containing the receptor-binding region in the amino terminal domain and a carboxyl terminal lipid-binding domain. Peptides derived from the LDL receptor (LDL-R)-binding region of apoE have been studied by a number of groups, with the primary focus being on the binding of the peptides to LDL-R. Based on the dual-domain structure, a peptide was designed with the highly cationic residues 141–150 from human apoE (hE) covalently bound to the lipid-associating class A α-helical peptide 18A and the amino and carboxyl termini blocked with acetyl and amide groups, respectively. This peptide, called Ac-hE18A-NH2 (in clinical development as AEM-28), was found to have striking cholesterol- and triglyceride-reducing and anti-inflammatory properties. Unlike statin drugs and proprotein convertase subtilisin/kexin type-9 (PCSK-9) inhibitors, these properties exist even in the absence of a functional LDL-R, with cholesterol reduction being mediated by binding to heparan sulfate proteoglycans (HSPG). Ac-hE18A-NH2 is currently undergoing phase 1a/1b clinical trials and has shown acceptable tolerability and promising efficacy. Thus, this and similar peptides have great potential for treatment of statin-resistant conditions such as familial hypercholesterolemia and acute hypertriglyceridemic pancreatitis.

Conflicts of Interest 

LipimetiX Development LLC has licensed the peptide described in this study, and Dennis Goldberg is president of this company. All authors have intellectual property in these peptides.

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Authors and Affiliations

  1. Department of Medicine, University of Alabama at Birmingham, BDB Room D-654, 1720 2nd Ave S, Birmingham, AL, 35294-0012, USA

    David W. Garber

  2. LipimetiX Development LLC, 5 Commonwealth Rd, Suite 2A, Natick, MA, USA

    Dennis Goldberg

  3. Department of Medicine, Department of Biochemistry and Molecular Biology, University of Alabama at Birmingham, Birmingham, AL, USA

    G. M. Anantharamaiah

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  1. David W. Garber
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  2. Dennis Goldberg
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  3. G. M. Anantharamaiah
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Correspondence to David W. Garber .

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Editors and Affiliations

  1. Department of Medicine, University of Alabama School of Medicine, Birmingham, Alabama, USA

    G.M. Anantharamaiah

  2. LipimetiX Development, LLC, Natick, Massachusetts, USA

    Dennis Goldberg

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Garber, D.W., Goldberg, D., Anantharamaiah, G.M. (2015). Apolipoprotein E Mimetic Peptides: Cholesterol-Dependent and Cholesterol-Independent Properties. In: Anantharamaiah, G., Goldberg, D. (eds) Apolipoprotein Mimetics in the Management of Human Disease. Adis, Cham. https://doi.org/10.1007/978-3-319-17350-4_10

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