Caspase-3-Responsive, Fluorogenic Bivalent Bottlebrush Polymers
Name
nihms-2097264.pdf
Description
Accepted version
Size
1.17 MB
Format
Adobe PDF
Checksum (MD5)
1d478575819d1b4f05410e2c189a2869
Author(s)
Zafar, Hadiqa
Liu, Bin
Nguyen, Hung V-T
Johnson, Jeremiah A
Date Issued
April 22, 2024
Journal
ACS Macro Letters
Publisher
American Chemical Society
Citation
Hadiqa Zafar, Bin Liu, Hung V.-T. Nguyen, Jeremiah A. Johnson; Caspase-3-Responsive, Fluorogenic Bivalent Bottlebrush Polymers. ACS Macro Lett. 21 May 2024; 13 (5): 571–576.
Version
Author's final manuscript
Abstract
Controlling the access of proteases to cleavable peptides placed at specific locations within macromolecular architectures represents a powerful strategy for biologically responsive materials design. Here, we report the synthesis of peptide-containing bivalent bottlebrush (co)polymers (BBPs) featuring polyethylene glycol (PEG) and 7-amino-4-methylcoumarin (AMC) pendants on each backbone repeat unit. The AMCs are linked via caspase-3-cleavable peptides which, upon enzymatic cleavage, provide a "turn-on" fluorescence signal due to the release of free AMC. Time-dependent fluorscence measurements demonstrate that the caspase-3-induced peptide cleavage and AMC release from BBPs is strongly dependent on the BBP backbone length and the AMC-peptide linker location within the BBP architecture, revealing fundamental insights into the interactions of enzymes with BBPs.
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DOI of Published Version
https://doi.org/10.1021/acsmacrolett.4c00119
