Integrin targeting fluorescent proteins: exploration of RGD insertion sites

M. Sonntag, J. Schill, L. Brunsveld (Corresponding author)

Research output: Contribution to journalArticleAcademicpeer-review

4 Citations (Scopus)
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Abstract

The potential of the fluorescent protein scaffold in controlling peptide sequence functionality is illustrated via the exploration of fluorescent proteins as novel probes for targeting of integrins. A library of fluorescent mCitrine proteins with RGD motifs incorporated at several positions in loops within the protein main chain was generated and characterized. Amino acid mutations to RGD as well as RGD motif insertions were evaluated and both approaches led to mCitrine constructs with typical fluorescent properties. Screening experiments against four human integrin receptors revealed two strong binding constructs and two selective integrin binders. The importance of the site of RGD incorporation illustrates the effect of the protein scaffold on RGD sequence functionality, leading to fluorescent protein constructs with the potential for selective integrin targeting.

Original languageEnglish
Pages (from-to)441–443
Number of pages3
JournalChemBioChem
Volume18
Issue number5
Early online date22 Dec 2016
DOIs
Publication statusPublished - 2 Mar 2017

Keywords

  • RGD
  • fluorescent probes
  • integrin
  • protein engineering
  • protein-protein interactions
  • Humans
  • Integrins/chemistry
  • Oligopeptides/chemistry
  • Fluorescent Dyes/chemistry
  • Genetic Variation
  • Protein Engineering
  • Protein Binding
  • Binding Sites

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