Design and synthesis of multiple-loop receptors based on a calix[4] arene scaffold for protein surface recognition

Research output: Contribution to journalArticle

Abstract

We have recently reported a synthetic protein binding agent with fourfold symmetry containing four identical peptide loops attached to the four phenyl groups of a calix[4]arene core. One of these first generation derivatives not only bound strongly to cytochrome c but also blocked its ability to interact with protein partners or simple reducing agents. In developing second generation protein binding agents with better affinity and selectivity, we required a synthetic approach that would lead to a less symmetrical arrangement of the peptide loops around the core calix[4]arene scaffold. We herein report an important step in the wider application of this strategy with the preparation of a series of unsymmetrical receptors in which two different loops are attached to the core calixarene.

Original languageEnglish (US)
Pages (from-to)441-450
Number of pages10
JournalComptes Rendus Chimie
Volume5
Issue number5
DOIs
StatePublished - Dec 1 2002

Keywords

  • Cali[4]arene
  • Protein recognition

ASJC Scopus subject areas

  • Chemistry(all)
  • Chemical Engineering(all)

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