The Membrane Penetrating Ability of Opicalcin1 Is Mainly Derived from the Latter Segment in Its Primary Sequence

Povilaitis, S. and Webb, L., Leaflet-dependent effect of anionic lipids on membrane insertion by cationic cell-penetrating peptides, J. Phys. Chem. Lett., 2023, vol. 14, no. 25, pp. 5841–5849. https://doi.org/10.1021/acs.jpclett.3c00725

Article  CAS  PubMed  PubMed Central  Google Scholar 

Guidotti, G., Brambilla, L., and Rossi, D., Cell-penetrating peptides: From basic research to clinics, Trends Pharmacol. Sci., 2017, vol. 38, no. 4, pp. 406–424. https://doi.org/10.1016/j.tips.2017.01.003

Article  CAS  PubMed  Google Scholar 

Reissmann, S., Cell penetration: Scope and limitations by the application of cell-penetrating peptides, J. Pept. Sci., 2014, vol. 20, no. 10, pp. 760–784. https://doi.org/10.1002/psc.2672

Article  CAS  PubMed  Google Scholar 

Ruseska, I. and Zimmer, A., Internalization mechanisms of cell-penetrating peptides, Beilstein J. Nanotechnol., 2020, vol. 11, pp. 101–123. https://doi.org/10.3762/bjnano.11.10

Article  CAS  PubMed  PubMed Central  Google Scholar 

Mabrouk, K., Ram, N., Boisseau, S., et al., Critical amino acid residues of maurocalcine involved in pharmacology, lipid interaction and cell penetration, Biochim. Biophys. Acta, 2007, vol. 1768, no. 10, pp. 2528–2540. https://doi.org/10.1016/j.bbamem.2007.06.030

Article  CAS  PubMed  Google Scholar 

Woll, K., Haji-Ghassemi, O., and Van Petegem, F., Pathological conformations of disease mutant Ryanodine Receptors revealed by cryo-EM, Nat. Commun., 2021, vol. 12, no. 1, p. 807. https://doi.org/10.1038/s41467-021-21141-3

Article  ADS  CAS  PubMed  PubMed Central  Google Scholar 

Caliskan, F., Quintero-Hernández, V., Restano-Cassulini, R., et al., Molecular cloning and biochemical characterization of the first Na(+)-channel alpha-type toxin peptide (Acra4) from Androctonus crassicauda scorpion venom, Biochimie, 2013, vol. 95, no. 6, pp. 1216–1222. https://doi.org/10.1016/j.biochi.2013.01.015

Article  CAS  PubMed  Google Scholar 

Lin King, J.V., Emrick, J.J., Kelly, M.J.S., et al., A cell-penetrating scorpion toxin enables mode-specific modulation of TRPA1 and pain, Cell, 2019, vol. 178, no. 6, pp. 1362–1374. https://doi.org/10.1016/j.cell.2019.07.014

Article  CAS  PubMed  PubMed Central  Google Scholar 

Valdivia, H. and Possani, L., Peptide toxins as probes of ryanodine receptor structure and function, Trends Cardiovasc. Med., 1998, vol. 8, no. 3, pp. 111–118. https://doi.org/10.1016/S1050-1738(97)00138-2

Article  CAS  PubMed  Google Scholar 

Xiao, L., Gurrola, G.B., Zhang, J., et al., Structure-function relationships of peptides forming the calcin family of ryanodine receptor ligands, J. Gen. Physiol., 2016, vol. 147, no. 5, pp. 375–394. https://doi.org/10.1085/jgp.201511499

Article  CAS  PubMed  PubMed Central  Google Scholar 

Kardani, K. and Bolhassani, A., Cppsite 2.0: An available database of experimentally validated cell-penetrating peptides predicting their secondary and tertiary structures, J. Mol. Biol., 2021, vol. 433, no. 11, p. 166703. https://doi.org/10.1016/j.jmb.2020.11.002

Article  CAS  PubMed  Google Scholar 

Ye, J., Liu, E., Gong, J., et al., High-yield synthesis of monomeric LMWP(CPP)-siRNA covalent conjugate for effective cytosolic delivery of siRNA, Theranostics, 2017, vol. 7, no. 9, pp. 2495–2508. https://doi.org/10.7150/thno.19863

Jumper, J., Evans, R., Pritzel, A., et al., Highly accurate protein structure prediction with AlphaFold, Nature, 2017, vol. 596, no. 7873, pp. 583–589. https://doi.org/10.1038/s41586-021-03819-2

Article  ADS  CAS  Google Scholar 

Ali, A., Mishra, R., Kaur, H., and Chandra Banerjea, A., HIV-1 Tat: An update on transcriptional and non-transcriptional functions, Biochimie, 2021, vol. 190, pp. 24–35. https://doi.org/10.1016/j.biochi.2021.07.001

Article  CAS  PubMed  Google Scholar 

Danielsen, E.M. and Hansen, G.H., Impact of cell-penetrating peptides (CPPs) melittin and Hiv-1 Tat on the enterocyte brush border using a mucosal explant system, Biochim. Biophys. Acta, Biomembr., 2018, vol. 1860, no. 8, pp. 1589–1599. https://doi.org/10.1016/j.bbamem.2018.05.015

Article  CAS  Google Scholar 

Perret, P., Ahmadi, M., Riou, L., Bacot, S., Pecher, J., Poillot, C., Broisat, A., Ghezzi, C., and De Waard, M., Biodistribution, stability, and blood distribution of the cell penetrating peptide maurocalcine in mice, Int. J. Mol. Sci., 2015, vol. 16, no. 11, pp. 27730–27740. https://doi.org/10.3390/ijms161126054

Article  CAS  PubMed  PubMed Central  Google Scholar 

Khamehchian, S., Nikkhah, M., Madani, R., and Hosseinkhani, S., Enhanced and selective permeability of gold nanoparticles functionalized with cell penetrating peptide derived from maurocalcine animal toxin, J. Biomed. Mater. Res., Part A, 2016, vol. 104, no. 11, pp. 2693–2700. https://doi.org/10.1002/jbm.a.35806

Article  CAS  Google Scholar 

Derossi, D., Joliot, A.H., Chassaing, G., and Prochiantz, A., The third helix of the Antennapedia homeodomain translocates through biological membranes, J. Biol. Chem., 1994, vol. 269, no. 14, pp. 10444–10450.

Article  CAS  PubMed  Google Scholar 

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