Synthetic antibody mimics for the inhibition of protein-ligand interactions

Curr Opin Chem Biol. 2017 Oct:40:72-77. doi: 10.1016/j.cbpa.2017.07.001. Epub 2017 Sep 18.

Abstract

The rational/structure-based design and/or combinatorial development of molecules capable of selectively binding to a protein, represents a promising strategy for a range of biomedical applications, in particular the inhibition of disease-associated protein-ligand interactions. The design of such protein binding molecules is often based on an antibody against the target protein, or involves the generation of smaller molecules that retain the binding characteristics of the antibody. Alternatively, protein binding molecules can be selected from protein libraries based on small, stably folded protein scaffolds presenting flexible loops, which are randomized in the libraries. In addition to recombinantly synthesized molecules, synthetic antibody paratope mimetic peptides have emerged as promising molecules for the design of antibody mimics.

Publication types

  • Review

MeSH terms

  • Animals
  • Aptamers, Nucleotide / chemistry
  • Aptamers, Nucleotide / metabolism
  • Aptamers, Nucleotide / pharmacology*
  • Humans
  • Immunoglobulin Fab Fragments / chemistry
  • Immunoglobulin Fab Fragments / metabolism
  • Immunoglobulin Fab Fragments / pharmacology*
  • Ligands
  • Models, Molecular
  • Peptidomimetics / chemistry
  • Peptidomimetics / metabolism
  • Peptidomimetics / pharmacology*
  • Protein Binding / drug effects
  • Proteins / chemistry
  • Proteins / metabolism*
  • Single-Chain Antibodies / chemistry
  • Single-Chain Antibodies / metabolism
  • Single-Chain Antibodies / pharmacology*
  • Single-Domain Antibodies / chemistry
  • Single-Domain Antibodies / metabolism
  • Single-Domain Antibodies / pharmacology*

Substances

  • Aptamers, Nucleotide
  • Immunoglobulin Fab Fragments
  • Ligands
  • Peptidomimetics
  • Proteins
  • Single-Chain Antibodies
  • Single-Domain Antibodies