期刊
NANO LETTERS
卷 20, 期 10, 页码 7375-7381出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.nanolett.0c02781
关键词
peptide nanofibers; cathepsin B; enzymatic degradation; internal viscosity; molecular rotors; fluorescence lifetime imaging
类别
资金
- Seed Award in Science by the Wellcome Trust [210122/Z/18/Z]
- EPSRC [EP/I003983/1]
- Excellence Fund for Frontier Research, Imperial College London
- Wellcome Trust [210122/Z/18/Z] Funding Source: Wellcome Trust
- EPSRC [EP/I003983/1] Funding Source: UKRI
Enzyme-responsive supramolecular peptide biomaterials have attracted growing interest for disease diagnostics and treatments. However, it remains unclear whether enzymes target the peptide assemblies or dissociated peptide monomers. To gain further insight into the degradation mechanism of supramolecular peptide amphiphile (PA) nanofibers, cathepsin B with both exopeptidase and endopeptidase activities was exploited here for degradation studies. Hydrolysis was found to occur directly on the PA nanofibers as only surface amino acid residues were cleaved. The number of cleaved residues and the degradation efficiency was observed to be negatively correlated with the internal viscosity of the PA nanofibers, quantified to be between 200-800 cP (liquid phase) using fluorescence lifetime imaging microscopy combined with an environmentally sensitive molecular rotor, BODIPY-C10. These findings enhance our understanding on the enzymatic degradation of supramolecular PA nanofibers and have important implications for the development of PA probes for the real-time monitoring of disease-related enzymes.
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