Journal
NANO LETTERS
Volume 21, Issue 14, Pages 6202-6210Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.nanolett.1c01950
Keywords
peptides; binding-induced fibrillogenesis; vimentin; self-assembly; tumor metastasis
Categories
Funding
- National Key R&D Program of China [2018YFE0205400]
- National Natural Science Foundation of China [51890891, 51890892, 51890894, 51725302, 51573031, 51573032]
- Science Fund for Creative Research Groups of the National Natural Science Foundation of China [11621505]
- CAS Interdisciplinary Innovation Team
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The study introduces a BIF peptide that inhibits the improper self-assembly of vimentin in cancer cells, reducing migration and invasion. In mouse models of tumor metastasis, the BIF peptide shows higher efficacy compared to small molecular inhibitors.
Life is recognized as a sophisticated self-assembling material system. Cancer involves the overexpression and improper self-assembly of proteins, such as cytoskeleton protein vimentin, an emerging target related to tumor metastasis. Herein, we design a binding-induced fibrillogenesis (BIF) peptide that in situ forms fibrous networks, blocking the improper self-assembly of vimentin against cancer. The BIF peptide can bind to vimentin and subsequently perform fibrillogenesis to form fibers on vimentin. The resultant peptide fibrous network blocks vimentin skeletonization and inhibits the migration and invasion of tumor cells. In mouse models of tumor metastasis, the volume of tumor and the number of lung metastases are markedly decreased. Moreover, the efficacy of BIF peptide (5 mg/kg) is much higher than small molecular antimetastasis drug withaferin A (5 mg/kg) as a standard, indicating that the BIF peptide shows advantages over small molecular inhibitors in blocking the intracellular protein self-assembly.
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