Biomimetic conformation-specific assembly of proteins at artificial binding sites nanopatterned on silicon

Roberto De La Rica, Hiroshi Matsui

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

Biomolecules such as enzymes and antibodies possess binding sites where the molecular architecture and the physicochemical properties are optimum for their interaction with a particular target, in some cases even differentiating between stereoisomers. Here, we mimic this exquisite specificity via the creation of a suitable chemical environment by fabricating artificial binding sites for the protein calmodulin (CaM). By downscaling well-known surface chemical modification methodologies to the nanometer scale via silicon nanopatterning, the Ca(2+)-CaM conformer was found to selectively bind the biomimetic binding sites. The methodology could be adapted to mimic other protein-receptor interactions for sensing and catalysis.
Original languageEnglish
Pages (from-to)14180–14181
Number of pages2
JournalJournal of the American Chemical Society
Volume131
Issue number40
DOIs
Publication statusPublished - 16 Sep 2009

Keywords

  • molecular architecture
  • binding sites
  • artificial binding

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