Biomimetic conformation-specific assembly of proteins at artificial binding sites nanopatterned on silicon.
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.
de la Rica
Roberto
R
Department of Chemistry and Biochemistry, City University of New York, Hunter College, 695 Park Avenue, New York, New York 10065, USA. roberto.delarica@gmail.com
Matsui
Hiroshi
H
D001665:Binding Sites; D040761:Biomimetic Materials / Q000737:chemistry*; D002147:Calmodulin / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D053758:Nanoparticles / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation; D012825:Silicon / Q000737:chemistry*; D013379:Substrate Specificity
D002147:Calmodulin; D012825:Silicon