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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 ASEP0565892
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleMitochondrial 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 authors9
    Source TitleACS Applied Materials and Interfaces. - : American Chemical Society - ISSN 1944-8244
    Roč. 13, č. 30 (2021), s. 35281-35293
    Number of pages13 s.
    Languageeng - English
    CountryUS - United States
    KeywordsVDAC1-derived amphiphilic peptides ; self-assembly ; mitochondria-mediated apoptosis ; targeting VDAC1−HK-II complex ; protein−protein interaction inhibit
    Subject RIVBF - Elementary Particles and High Energy Physics
    OECD categoryParticles and field physics
    R&D ProjectsEF15_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 publishingLimited access
    Institutional supportFZU-D - RVO:68378271
    UT WOS000683741400004
    EID SCOPUS85112524976
    DOI10.1021/acsami.1c04385
    AnnotationTargeted 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.
    WorkplaceInstitute of Physics
    ContactKristina Potocká, potocka@fzu.cz, Tel.: 220 318 579
    Year of Publishing2023
    Electronic addresshttps://doi.org/10.1021/acsami.1c04385
Number of the records: 1  

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