References
1. Fire A., Xu S., Montgomery M., Kostas S., Driver S., Mello C. Potent and specific genetic interference by double-stranded RNA in Caenorhabditis elegans. Nature. 1998; 391: 806–11. DOI: https://doi.org/10.1038/35888
2. Milletti F. Cell-penetrating peptides: classes, origin, and current landscape. Drug Discovery Today. 2012; 17: 850–60. DOI: https://doi.org/10.1016/j.drudis.2012.03.002
3. Luo K., Li C., Wang G., Nie Y., He B., Wu Y., Gu Z. Peptide dendrimers as efficient and biocompatible gene delivery vectors: Synthesis and in vitro characterization. J Control Rel. 2011; 55 (1): 77–87. DOI: https://doi.org/10.1016/j.jconrel.2010.10.006
4. Takechi-Haraya Y., Saito H. Current understanding of physicochemical mechanisms for cell membrane penetration of arginine-rich cell penetrating peptides: role of glycosaminoglycan Interactions. Curr Prot Pept Sci. 2018; 19 (6): 623–30. DOI: https://doi.org/10.1016/j.jconrel.2010.10.006
5. Kumar V., Agrawal P., Kumar R., Bhalla S., Usmani S.S., Varshney G.C., Raghava G. P. Prediction of cell-penetrating potential of modified peptides containing natural and chemically modified residues. Front Мicrobiоl. 2018; 9: 725. DOI: https://doi.org/10.3389/fmicb.2018.00725
6. Hofland H.E., Shephard L., Sullivan S.M. Formation of stable cationic lipid/DNA complexes for gene transfer. Proc Natl Acad Sci. USA. 1996; 93: 7305–9.
7. Turetsky E.A., Koloskova O.O., Nosova A.S., Shilovsky I.P., Sebyakin Yu.L., Khaitov M.R. Physicochemical properties of lipopeptide-based liposomes and their complexes with siRNA. Biomedical Chemistry. 2017; 63 (5): 472–5. DOI: https://doi.org/10.18097/PBMC20176305472 (in Russian)
8. Regberg J., Srimanee A., Erlandsson M., Sillard R., Dobchev D.A., Karelson M., Langel U. Rational design of a series of novel amphipathic cell-penetrating peptides. Int J Pharm. 2014; 464 (1-2): 111–6. DOI: https://doi.org/10.1016/j.ijpharm.2014.01.018
9. Eggimann G.A., Blattes E., Buschor S., Biswas R., Kammer S.M., Darbre T., Reymond J.-L. Designed cell penetrating peptide dendrimers efficiently internalize cargo into cells. Chem Comm. 2014; 50: 7254. DOI: https://doi.org/10.1039/C4CC02780A
10. Shcharbin D., Shcharbina N., Bryszewska M. Recent patents in dendrimers for nanomedicine: Evolution 2014. Recent patents on nanomedicine. 2014; 4 (1): 25–31. DOI: https://doi.org/10.2174/1877912304666140609233256
11. Nikolskii A.A., Shilovskiy I.P., Yumashev K.V., Vishniakova L.I., Barvinskaia E.D., Kovchina V.I., Korneev A.V., Turenko V.N., Kaganova M.M., Brylina V.E., Nikonova A.A., Kozlov I.B., Kofiadi I.A., Sergeev I.V., Maerle A.V., Petukhova O.A., Kudlay D.A., Khaitov M.R. Effect of local suppression of Stat3 gene expression in a mouse model of pulmonary neutrophilic inflammation. Immunologiya. 2021; 42 (6): 600–14. DOI: https://doi.org/10.33029/0206-4952-2021-42-6-600-614 (in Russian)
12. Kozhikhova K.V., Andreev S.M., Shilovskiy I.P., Timofeeva A.V., Gaisina A.R., Shatilov A.A., Turetskiy E.A., Andreev I.M., Smirnov V.V., Dvornikov A.S., Khaitov M.R. A novel peptide dendrimer LTP efficiently facilitates transfection of mammalian cells. Org Biomol Chem. 2018; 16 (43): 8181–90. DOI: https://doi.org/10.1039/C8OB02039F
13. Allolio C., Magarkar A., Jurkiewicz P., Baxová K., Javanainen M., Mason P.E., Šachl R., Cebecauer M., Hof M., Horinek D., Heinz V., Rachel R., Ziegler C.M., Schröfel A., Jungwirth P. Arginine-rich cell-penetrating peptides induce membrane multilamellarity and subsequently enter via formation of a fusion pore. Proc Natl Acad Sci USA. 2018; 115: 11923–8. DOI: https://doi.org/10.1073/pnas.1811520115
14. Takechi-Haraya1 Y., Ohgita T., Kotani M., Kono H., Saito C., Tamagaki-Asahina H., Nishitsuji K., Uchimura K., Sato T., Kawano R., Sakai-Kato K., Izutsu K., Saito H. Effect of hydrophobic moment on membrane interaction and cell penetration of apolipoprotein E-derived arginine-rich amphipathic α-helical peptides. Sci Reports. 2022; 12: 4959. DOI: https://doi.org/10.1038/s41598-022-08876-9
15. Mosmann T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J Immun Methods. 1983; 65: 55–63. DOI: https://doi.org/10.1016/0022-1759(83)90303-4
16. Frommel C. The apolar surface area of amino acids and its empirical correlation with hydrophobic free energy. J Theor Biol. 1984; 111: 247–260. DOI: https://doi.org/10.1016/S0022-5193(84)80209-X
17. Ponkratova D. A., Lushnikova A.A. Structural features and expression of NPM and NCL in cutaneous melanoma. Molecular Biology. 2019; 53 (4): 663–73. DOI: https://doi.org/10.1134/S0026898419040098 (in Russian)
18. Kozhikhova K.V., Shilovskiy I.P., Shatilov A.A., Timofeeva F.V., Turetskiy E.A., Vishniakova L.I., Nikolskii A.A., Barvinskaya E.D., Karthikeyan S., Smirnov V.V., Kudlay D.A., Andreev S.A., Khaitov M.R. Linear and dendrimeric antiviral peptides: Design, chemical synthesis and activity against human respiratory syncytial virus. J Mater Chem. B. 2020; 8: 2607–17. DOI: https://doi.org/10.1039/C9TB02485A
19. Feng Z., Xu L., Xie Z. Receptors for respiratory syncytial virus infection and host factors regulating the life cycle of respiratory syncytial virus. Front Cell Infect. Microbiol. 2022; 12: 858629. DOI: https://doi.org/10.3389/fcimb.2022.858629
20. Vazdar M., Heyda J., Mason P.E., Tesei J., Allolio C., Lund M., Jungwirth P. Arginine «magic»: Guanidinium like-charge ion pairing from aqueous salts to cell penetrating peptides. Acc. Chem. Res. 2018; 51: 1455−64. DOI: https://doi.org/10.1021/acs.accounts.8b00098
21. Chua B.Y., Zeng W., Jackson D.C. Simple branched arginine-based structures can enhance the cellular uptake of peptide cargos. Int J Pep Therap. 2007; 13 (3): 431–7. DOI: https://doi.org/10.1007/s10989-006-9063-y
22. Das U., Hariprasad G., Ethayathulla A.S., Manral P., Das T.K., Pasha S., Mann A., Ganguli M., Verma A.K., Bhat R., Chandrayan S.K., Ahmed S., Sharma S., Kaur P., Singh T.P., Srinivasan A. Inhibition of protein aggregation: Supramolecular assemblies of arginine hold the key. PLoS ONE. 2007; 2 (11): e1176. DOI: https://doi.org/10.1371/journal.pone.0001176
23. Huang J., Wang J., Li Y., Wang Z., Chu M., Wang Y. Tuftsin: A natural molecule against SARS-CoV-2 infection. Front Mol Biosci. 2022; 9: 859162. DOI: https://doi.org/10.3389/fmolb.2022.859162
24. Simeoni F., Morris M.C., Heitz F., Divita G. Insight into the mechanism of the peptide-based gene delivery system MPG: implications for delivery of siRNA into mammalian cells. NAR. 2003; 31 (11): 2717–24.
25. Fu Y., Chen Y., Luo X., Liang Y., Shi H., Gao L., Zhan S., Zhou D., Luo Y. The heparin binding motif of endostatin mediates its interaction with receptor nucleolin. Biochemistry. 2009; 48 (49): 11655–63. DOI: https://doi.org/10.1021/bi901265z
26. Lushnikova A.A., Morozova L.F., Pankratova D.A., Balbutsky A.V., Andreev S.M., Mikhailov A.E., Khaitov M.R. Application of cationic peptides for induction of human skin melanoma cell death. Patent. RU26 20170 C1
27. Khaitov M., Nikonova А., Shilovskiy I., Kozhikhova K., Kofiadi I., Vishnyakova L., Nikolsky A., Gattinger P., Kovchina V., Barvinskaya E., Yumashev K., Smirnov V., Maerle A., Kozlov I., Shatilov A., Timofeeva A., Andreev S., Koloskova O., Kuznetsova N., Vasina D., Nikiforova M., Rybalkin S., Sergeev I., Trofimov D., Martynov A., Berzin I., Gushchin I., Kovalchuk A., Borisevich S., Valenta R., Khaitov R., Skvortsova V. Silencing of SARS-CoV-2 with modified siRNA-peptide dendrimer formulation. Allergy. 2021; 76 (9): 2840–54. DOI: https://doi.org/10.1111/all.14850