{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zafar H"],"funding":["National Science Foundation Graduate Research Fellowship Program","National Cancer Institute","NCI NIH HHS"],"pagination":["571-576"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12323701"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13(5)"],"pubmed_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 <i>bivalent</i> 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 architectur"],"journal":["ACS macro letters"],"pubmed_title":["Caspase-3-Responsive, Fluorogenic Bivalent Bottlebrush Polymers."],"pmcid":["PMC12323701"],"funding_grant_id":["R01 CA220468","2R01CA220468-06A1"],"pubmed_authors":["Nguyen HV","Zafar H","Liu B","Johnson JA"],"additional_accession":[]},"is_claimable":false,"name":"Caspase-3-Responsive, Fluorogenic Bivalent Bottlebrush Polymers.","description":"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 <i>bivalent</i> 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 architectur","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 May","modification":"2026-03-31T11:48:52.604Z","creation":"2025-09-01T03:05:36.099Z"},"accession":"S-EPMC12323701","cross_references":{"pubmed":["38647178"],"doi":["10.1021/acsmacrolett.4c00119"]}}