Fig. 1

Recruitment of β-lactamase and BLIP on a supramolecular BTA polymer via DNA hybridization. a Schematic representation of the selective recruitment of proteins to BTA polymers. (i) BTA monomers functionalized with a 10-nucleotide handle strand (BTA-DNA) are co-assembled in a desired ratio with inert BTA monomers (BTA-3OH) to yield supramolecular polymers decorated with DNA receptors. (ii) To allow sequence specific oligonucleotide directed recruitment of the enzyme (β-lactamase) and its inhibitor protein (BLIP), each protein is functionalized with a unique 21-nucleotide handle strand. (iii) Addition of a specific recruiter oligonucleotide that is complementary to the handle strand on the BTA polymer and the enzyme (enzyme recruiter (R_E)), results in selective recruitment of the enzyme to the supramolecular polymer. (iv) Addition of the inhibitor recruiter strand (R_I) results in the recruitment of the inhibitor to the supramolecular platform. (v) The dynamic nature of the platform allows the rearrangement of the proteins along the polymer to allow enzyme-inhibitor complex formation, resulting in decreased enzyme activity. b The chemical structures of BTA-3OH and BTA-DNA. c The hydrolysis of a β-lactam-containing substrate which is catalyzed by β-lactamase