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Mitochondrial voltage-dependent anion channel 1–hexokinase-II complex-targeted strategy for melanoma inhibition using designed multiblock peptide amphiphiles
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SYSNO ASEP 0565892 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Mitochondrial voltage-dependent anion channel 1–hexokinase-II complex-targeted strategy for melanoma inhibition using designed multiblock peptide amphiphiles Author(s) Zhang, F. (CN)
Angelova, A. (FR)
Garamus, V. M. (DE)
Angelov, Borislav (FZU-D) ORCID
Tu, S. (CN)
Kong, L. (CN)
Zhang, X. (CN)
Li, N. (CN)
Zou, A. (CN)Number of authors 9 Source Title ACS Applied Materials and Interfaces. - : American Chemical Society - ISSN 1944-8244
Roč. 13, č. 30 (2021), s. 35281-35293Number of pages 13 s. Language eng - English Country US - United States Keywords VDAC1-derived amphiphilic peptides ; self-assembly ; mitochondria-mediated apoptosis ; targeting VDAC1−HK-II complex ; protein−protein interaction inhibit Subject RIV BF - Elementary Particles and High Energy Physics OECD category Particles and field physics R&D Projects EF15_003/0000447 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) EF16_019/0000789 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) Method of publishing Limited access Institutional support FZU-D - RVO:68378271 UT WOS 000683741400004 EID SCOPUS 85112524976 DOI 10.1021/acsami.1c04385 Annotation Targeted therapies of melanoma are of urgent need considering the resistance of this aggressive type of cancer to chemotherapeutics. The voltage-dependent anion channel 1 (VDAC1)–hexokinase-II (HK-II) complex is an emerging target for novel anticancer therapies based on induced mitochondria-mediated apoptosis. The low cell membrane permeability of the anticancer 12-mer peptide N-Ter (RDVFTKGYGFGL) derived from the N-terminal fragment of the VDAC1 protein impedes the intracellular targeting. Here, novel multiblock VDAC1-derived cationic amphiphilic peptides (referred to as Pal-N-Ter-TAT, pFL-N-Ter-TAT, and Pal-pFL-N-Ter-TAT) are designed with a self-assembly propensity and cell-penetrating properties. The created multiblock amphiphilic peptides of partial α-helical conformations form nanoparticles of ellipsoid-like shapes and are characterized by enhanced cellular uptake.
Workplace Institute of Physics Contact Kristina Potocká, potocka@fzu.cz, Tel.: 220 318 579 Year of Publishing 2023 Electronic address https://doi.org/10.1021/acsami.1c04385
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