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High-Affinity α5β1-Integrin-Selective Bicyclic RGD Peptides Identified via Screening of Designed Random Libraries.

Dominik Bernhagen1, Vanessa Jungbluth2, Nestor Gisbert Quilis2

  • 1Pepscan Therapeutics , Zuidersluisweg 2 , 8243 RC Lelystad , the Netherlands.

ACS Combinatorial Science
|July 4, 2019
PubMed
Summary
This summary is machine-generated.

We developed novel bicyclic peptides that bind selectively to integrin α5β1. These peptides demonstrate high affinity and potential as diagnostic markers for α5β1 expression.

Keywords:
ELISARGDSPFSbicyclic peptideintegrinlibrary screeningpeptide−protein interaction

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Drug Discovery

Background:

  • Integrin α5β1 plays a crucial role in cellular processes, including adhesion and migration.
  • Targeting integrins is a key strategy in developing therapeutics and diagnostics.

Purpose of the Study:

  • To identify high-affinity and selective bicyclic peptides that bind to integrin α5β1.
  • To evaluate the potential of these peptides as markers for α5β1 expression.

Main Methods:

  • Screening of designed random libraries containing the Arg-Gly-Asp (RGD) sequence.
  • Affinity and selectivity profiling using biochemical assays (IC50, Kd) and Surface Plasmon Resonance.
  • In vitro cell staining using confocal microscopy.

Main Results:

  • Identification of potent α5β1-binding bicyclic peptides with nanomolar affinity.
  • One identified peptide, CRGDcAYJ(d-Leu)C, exhibited higher affinity than the benchmark knottin-RGD.
  • Excellent selectivity over integrins αvβ5 and acceptable selectivity over αvβ3.
  • Demonstrated successful in vitro labeling of adipose-derived stem cells, highlighting potential as α5β1 markers.

Conclusions:

  • Designed random libraries are effective for discovering high-affinity integrin binders.
  • The identified RGD-bicyclic peptides are promising candidates for α5β1-targeted diagnostics and therapeutics.
  • These peptides can serve as valuable tools for visualizing α5β1 expression in biological systems.