Journal
BIOCONJUGATE CHEMISTRY
Volume 19, Issue 1, Pages 57-64Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bc070081p
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Funding
- NCI NIH HHS [1R01 CA113746] Funding Source: Medline
- NCRR NIH HHS [P20 RR016741] Funding Source: Medline
- NATIONAL CANCER INSTITUTE [R01CA113746] Funding Source: NIH RePORTER
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We offer a novel methodology for formulating liposomes by incorporating sequence-specific collagen-mimetic peptides such that they are specifically uncorked by a matrix metalloproteinase, MMP-9. By encapsulating carboxyfluorescein (as-a self-quenching fluorescent dye), we demonstrate that the time-dependent release of the dye from liposomes is due to the specific enzymatic cleavage of the surface-exposed collagen-mimetic peptides. The specificity of such cleavage is attested by the fact that the liposomal uncorking and their content release occur only by MMP-9 and not by a general proteolytic enzyme, trypsin, despite the fact that the collagen mimetic peptides contain the trypsin cleavage site. The mechanistic details underlying the formulations of liposomes and. their enzyme-selective uncorking and content release are discussed. Arguments are presented that such liposomes can be fine-tuned to serve as the drug delivery vehicles for the detection and treatment of various human diseases, which occur due to the overexpression of a variety of pathogenic matrix metalloproteinases.
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