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• Have superior plasma stability comparable to that of non-cleavable linkers
Cathepsin B in the lysosome cleaves the peptide bond between Cit-PAB of dipeptide linkers containing valine (Val)-citrulline (Cit) and p-aminobenzylalcohol (PAB). When PAB and a drug are binded covalently with carbamate bonds, the drug can be released by hydrolysis after cleavage of the peptide bond between Cit-PAB. Antibody-drug conjugates (ADCs) has been developed using this mechanism.
- Cathepsin B-labile dipeptide linkers for lysosomal release of doxorubicin from internalizing immunoconjugates: model studies of enzymatic drug release and antigen-specific in vitro anticancer activity.
- A cell-penetrating peptidic GRP78 ligand for tumor cell-specific prodrug therapy
- Effect of Attachment Site on Stability of Cleavable Antibody Drug Conjugates