Mitochondrial voltage-dependent anion channel 1–hexokinase-II complex-targeted strategy for melanoma inhibition using designed multiblock peptide amphiphiles

0565892 - FZÚ 2023 RIV US eng J - Článek v odborném periodiku
Zhang, F. - Angelova, A. - Garamus, V. M. - Angelov, Borislav - Tu, S. - Kong, L. - Zhang, X. - Li, N. - Zou, A.
Mitochondrial voltage-dependent anion channel 1–hexokinase-II complex-targeted strategy for melanoma inhibition using designed multiblock peptide amphiphiles.
ACS Applied Materials and Interfaces. Roč. 13, č. 30 (2021), s. 35281-35293. ISSN 1944-8244. E-ISSN 1944-8252
Grant CEP: GA MŠMT EF15_003/0000447; GA MŠMT EF16_019/0000789
Grant ostatní: OP VVV - ELIBIO(XE) CZ.02.1.01/0.0/0.0/15_003/0000447; OP VVV - ADONIS(XE) CZ.02.1.01/0.0/0.0/16_019/0000789
Institucionální podpora: RVO:68378271
Klíčová slova: VDAC1-derived amphiphilic peptides * self-assembly * mitochondria-mediated apoptosis * targeting VDAC1−HK-II complex * protein−protein interaction inhibit
Obor OECD: Particles and field physics
Impakt faktor: 10.383, rok: 2021
Způsob publikování: Omezený přístup
https://doi.org/10.1021/acsami.1c04385

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.

Trvalý link: https://hdl.handle.net/11104/0337369