Protease-Triggered Dispersion of Nanoparticle Assemblies

摘要

We have developed a simple and highly sensitive method to detect the presence of proteases. The efficacy of the design in generating NP dispersion upon enzyme action arises from a dual mechanism of simultaneous removal of attractive self-assembly groups and revelation of repulsive charged groups. The resulting high sensitivity is likely related to the more favorable thermodynamics of peptide hydrolysis when it is coupled to the irreversible process of charge-induced NP dispersion. The modular approach can be easily tailored for different proteases, as demonstrated here for thermolysin and nACT-PSA.