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HER2-targeted, enzyme-activated liposomes show superior in vivo efficacy in an ovarian cancer model. | LitMetric

AI Article Synopsis

  • * In this study, a novel liposomal delivery system was created that uses trastuzumab, an antibody, to help the liposomes enter HER2-positive cancer cells more efficiently.
  • * The design includes a protective PEG layer that is cleaved by specific enzymes in the tumor microenvironment, leading to greater destabilization of the liposomes and increased drug release, resulting in improved anticancer activity in animal models.

Article Abstract

Liposomes carrying chemotherapeutic drugs can accumulate passively in solid tumors at high levels. However, additional targeting of the liposomes towards e.g. receptors expressed on cancer cells may improve their interaction and therapeutic properties. In this study, we designed a liposomal delivery system, which utilizes the intrinsic characteristics of HER2-positive tumors to ensure efficient delivery of oxaliplatin to the cancer cells. On the liposome surface, trastuzumab, an antibody specific to the HER2 receptor, was shown to facilitate internalization by the cancer cells. A polyethylene glycol (PEG) layer on the liposome surface provides protection from mononuclear phagocyte system uptake. To optimize the interaction between liposomes and cancer cells, a protease-sensitive cleavable peptide linker was inserted at the base of each PEG. The PEG layer is then cleaved off by intra- and extracellular matrix metalloproteinases (MMPs) upon accumulation in the tumor. Our data demonstrate that the removal of PEG significantly destabilizes the liposomes and leads to substantial oxaliplatin release. The proposed beneficial effect of combining antibody-mediated internalization with MMP sensitivity was confirmed in a series of in vivo studies using ovarian cancer xenograft models. The results demonstrated that HER2-targeted MMP-sensitive liposomes have superior anticancer activity compared to non-targeted and non-cleavable liposomes.

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Source
http://dx.doi.org/10.1016/j.jconrel.2024.05.005DOI Listing

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