Dimerization of the Peptide CXCR4-Antagonist on Macromolecular and Supramolecular Protraction Arms Affords Increased Potency and Enhanced Plasma Stability

Bioconjug Chem. 2022 Apr 20;33(4):594-607. doi: 10.1021/acs.bioconjchem.2c00034. Epub 2022 Mar 16.

Abstract

Peptides are prime drug candidates due to their high specificity of action but are disadvantaged by low proteolytic stability. Here, we focus on the development of stabilized analogues of EPI-X4, an endogenous peptide antagonist of CXCR4. We synthesized macromolecular peptide conjugates and performed side-by-side comparison with their albumin-binding counterparts and considered monovalent conjugates, divalent telechelic conjugates, and Y-shaped peptide dimers. All constructs were tested for competition with the CXCR4 antibody-receptor engagement, inhibition of receptor activation, and inhibition of the CXCR4-tropic human immunodeficiency virus infection. We found that the Y-shaped conjugates were more potent than the parent peptide and at the same time more stable in human plasma, with a favorable outlook for translational studies.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Dimerization
  • HIV Infections*
  • HIV-1* / physiology
  • Humans
  • Peptides / chemistry
  • Peptides / pharmacology
  • Receptors, CXCR4 / metabolism
  • Signal Transduction

Substances

  • CXCR4 protein, human
  • Peptides
  • Receptors, CXCR4