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

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.

SUBMITTER: de la Rica R

PROVIDER: S-EPMC2774499 | biostudies-literature | 2009 Oct

REPOSITORIES: biostudies-literature

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

de la Rica Roberto R Matsui Hiroshi H

Journal of the American Chemical Society 20091001 40

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 nan ...[more]

PMID: 19757782

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