Small Cause, Great Impact: Modification of the Guanidine Group in the RGD Motif Controls Integrin Subtype Selectivity

  • Tobias G. Kapp
  • , Maximilian Fottner
  • , Oleg V. Maltsev
  • , Horst Kessler

Research output: Contribution to journalArticlepeer-review

26 Scopus citations

Abstract

Due to its unique role as a hydrogen-bond donor and its positive charge, the guanidine group is an important pharmacophoric group and often used in synthetic ligands. The chemical modification of the guanidine group is often considered to destroy its function. Herein, we show that the N-methylation, N-alkylation, or N-acylation of the guanidine group can be used to modify the receptor subtype specificity of the integrin ligand cilengitide. Using the αvβ6/α5β1-biselective ligand c(isoDGRkphg) and the αvβ6-specific ligand c(FRGDLAFp(NMe)K(Ac) as examples, we show that the binding affinities of the ligands can be fine-tuned by this method to enhance the selectivity for αvβ6. Furthermore, we describe a new strategy for the functionalization of integrin ligands. By introducing longer N-alkylguanidine and N-acylguanidine groups, we are able to simultaneously identify a hitherto unknown anchoring point and enhance the subtype selectivity of the ligand.

Original languageEnglish
Pages (from-to)1540-1543
Number of pages4
JournalAngewandte Chemie International Edition in English
Volume55
Issue number4
DOIs
StatePublished - 22 Jan 2016

Keywords

  • RGD motif
  • cilengitide
  • integrin ligands
  • peptide modifications
  • receptor subtype selectivity

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