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.
- molecular architecture
- binding sites
- artificial binding
De La Rica, R., & Matsui, H. (2009). Biomimetic conformation-specific assembly of proteins at artificial binding sites nanopatterned on silicon. Journal of the American Chemical Society, 131(40), 14180–14181. https://doi.org/10.1021/ja905932e