AI Article Synopsis
- Enzyme activity relies on the specific interaction of substrates and their transformation, and traditional methods to enhance this activity often lack fine-tuned control over key variables.* -
- The study introduces a novel approach by colocalizing aptamers and enzymes in virus-like particles to improve catalytic efficiency through concentrated substrate availability.* -
- Results indicate that optimal catalytic performance occurs when the ratio of aptamers to enzymes is balanced, but excessive binding strength or insufficient proximity between aptamers and the enzyme can hinder effectiveness.*
Article Abstract
Enzyme activity requires sequential binding and chemical transformation of substrates. While directed evolution and random mutagenesis are common methods for improving catalytic activity, these methods do not allow for independent control of and . To achieve such control, we envisioned that the colocalization of aptamers and enzymes that act on the same molecule could increase catalytic efficiency through preconcentration of substrate. We explored this concept with cocaine esterase and anticocaine aptamers having varying values, both encapsulated in MS2 virus-like particles. Rate enhancements were observed with magnitudes dependent on both aptamer:enzyme stoichiometry and aptamer , peaking when aptamer and enzyme were roughly equivalent. This beneficial effect was lost when either aptamer binding was too tight or the aptamers were not constrained to be close to the catalyst. This work demonstrates a modular way to enhance catalysis by independently controlling substrate capture and release to the processing enzyme.
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| http://dx.doi.org/10.1021/acs.biomac.3c00144 | DOI Listing |
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