Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/97877
Title: Enzyme-responsive nanoparticles for drug release and diagnostics
Authors: Rica, Roberta de la
Aili, Daniel
Stevens, Molly M.
Issue Date: 2012
Source: Rica, R. d. l. R., Aili, D., & Stevens, M. M. (2012). Enzyme-responsive nanoparticles for drug release and diagnostics. Advanced Drug Delivery Reviews, 64(11), 967-978.
Series/Report no.: Advanced drug delivery reviews
Abstract: Enzymes are key components of the bionanotechnology toolbox that possess exceptional biorecognition capabilities and outstanding catalytic properties. When combined with the unique physical properties of nanomaterials, the resulting enzyme-responsive nanoparticles can be designed to perform functions efficiently and with high specificity for the triggering stimulus. This powerful concept has been successfully applied to the fabrication of drug delivery schemes where the tissue of interest is targeted via release of cargo triggered by the biocatalytic action of an enzyme. Moreover, the chemical transformation of the carrier by the enzyme can also generate therapeutic molecules, therefore paving the way to design multimodal nanomedicines with synergistic effects. Dysregulation of enzymatic activity has been observed in a number of severe pathological conditions, and this observation is useful not only to program drug delivery in vivo but also to fabricate ultrasensitive sensors for diagnosing these diseases. In this review, several enzyme-responsive nanomaterials such as polymer-based nanoparticles, liposomes, gold nanoparticles and quantum dots are introduced, and the modulation of their physicochemical properties by enzymatic activity emphasized. When known, toxicological issues related to the utilization nanomaterials are highlighted. Key examples of enzyme-responsive nanomaterials for drug delivery and diagnostics are presented, classified by the type of effector biomolecule, including hydrolases such as proteases, lipases and glycosidases, and oxidoreductases.
URI: https://hdl.handle.net/10356/97877
http://hdl.handle.net/10220/12349
ISSN: 0169-409X
DOI: http://dx.doi.org/10.1016/j.addr.2012.01.002
Rights: © 2012 Elsevier B.V.
Fulltext Permission: none
Fulltext Availability: No Fulltext
Appears in Collections:MSE Journal Articles

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