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

Roberto De La Rica, Hiroshi Matsui

Research output: Contribution to journalArticle

5 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.
LanguageEnglish
Pages14180–14181
Number of pages2
JournalJournal of the American Chemical Society
Volume131
Issue number40
DOIs
Publication statusPublished - 16 Sep 2009

Fingerprint

Biomimetics
biomimetics
Silicon
Binding sites
Calmodulin
calmodulin
Conformations
assembly
Binding Sites
Antibody Binding Sites
proteins
Proteins
Stereoisomerism
silicon
Catalysis
methodology
Carrier Proteins
Chemical modification
Biomolecules
antibodies

Keywords

  • molecular architecture
  • binding sites
  • artificial binding

Cite this

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Biomimetic conformation-specific assembly of proteins at artificial binding sites nanopatterned on silicon. / De La Rica, Roberto; Matsui, Hiroshi.

In: Journal of the American Chemical Society, Vol. 131, No. 40, 16.09.2009, p. 14180–14181.

Research output: Contribution to journalArticle

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AU - De La Rica, Roberto

AU - Matsui, Hiroshi

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AB - 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.

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KW - binding sites

KW - artificial binding

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