Journal
SUPRAMOLECULAR CHEMISTRY
Volume 31, Issue 10, Pages 676-683Publisher
TAYLOR & FRANCIS LTD
DOI: 10.1080/10610278.2019.1658874
Keywords
Bovine serum albumin; cucurbit[7]uril; switchable peptide probe; cell-penetrating peptide; matrix metalloproteinases 2
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Funding
- Science and Technology Planning Project of Taicang [TC2018JC03, TC2018JC04, TC2013YY03]
- National Natural Science Foundation of China [81703088]
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Herein, we develop a switchable peptide-equipped protein/cucurbit[7]uril (CB[7]) supramolecular assembly as novel targeted drug vector. Specifically, bovine serum albumin (BSA) is used to interact with CB[7], serving as the core of drug vector. Then, a peptide shield layer is formed on the surface of BSA/CB[7], yielding peptide-equipped supramolecular assembly (Pep@BSA@CB[7]). The equipped peptide shield layer is composed of switchable peptide probes consisting of a polycationic cell-penetrating peptide (CPP) motif, a polyanionic motif and a linking motif, and therefore provides a variety of desirable properties. First, the CPP motif displays excellent cell penetration ability and can facilitate internalisation of the drug vector. Secondly, the polyanionic motif performs intramolecular electrostatic interaction with CPP motif and thereby can reduce non-targeted delivery towards normal cells. Thirdly, the linking motif can be specifically cleaved by matrix metalloproteinases 2 that is up-regulated in tumour microenvironment, thus enabling precise cancer-targeting. As a consequent, Pep@BSA@CB[7] can serve as a promising drug vector that exhibits superior targeting ability and high uptake efficiency towards cancer cells, which may be of great potential in cancer-targeted treatment.
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