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Volumn 106, Issue , 2016, Pages 172-182

Peptides for nucleic acid delivery

Author keywords

Antisense oligonucleotides; Cell penetrating peptides; Delivery peptides; Nanoparticles; Nucleic acid delivery; Oligonucleotides; siRNA; Splice switching oligonucleotides

Indexed keywords

BIOCHEMISTRY; BIOMOLECULES; CELL CULTURE; GENE THERAPY; NANOPARTICLES; NUCLEIC ACIDS; OLIGONUCLEOTIDES; PEPTIDES;

EID: 84994885261     PISSN: 0169409X     EISSN: 18728294     Source Type: Journal    
DOI: 10.1016/j.addr.2016.06.008     Document Type: Review
Times cited : (187)

References (123)
  • 1
    • 84856431819 scopus 로고    scopus 로고
    • RNA therapeutics: beyond RNA interference and antisense oligonucleotides
    • [1] Kole, R., Krainer, A.R., Altman, S., RNA therapeutics: beyond RNA interference and antisense oligonucleotides. Nat. Rev. Drug Discov. 11 (2012), 125–140, 10.1038/nrd3625.
    • (2012) Nat. Rev. Drug Discov. , vol.11 , pp. 125-140
    • Kole, R.1    Krainer, A.R.2    Altman, S.3
  • 2
    • 79960981599 scopus 로고    scopus 로고
    • Targeting RNA to treat neuromuscular disease
    • [2] Muntoni, F., Wood, M.J.A., Targeting RNA to treat neuromuscular disease. Nat. Rev. Drug Discov. 10 (2011), 621–637, 10.1038/nrd3459.
    • (2011) Nat. Rev. Drug Discov. , vol.10 , pp. 621-637
    • Muntoni, F.1    Wood, M.J.A.2
  • 3
    • 77949512140 scopus 로고    scopus 로고
    • RNA targeting therapeutics: molecular mechanisms of antisense oligonucleotides as a therapeutic platform
    • [3] Bennett, C.F., Swayze, E.E., RNA targeting therapeutics: molecular mechanisms of antisense oligonucleotides as a therapeutic platform. Annu. Rev. Pharmacol. Toxicol. 50 (2010), 259–293, 10.1146/annurev.pharmtox.010909.105654.
    • (2010) Annu. Rev. Pharmacol. Toxicol. , vol.50 , pp. 259-293
    • Bennett, C.F.1    Swayze, E.E.2
  • 4
    • 82755161958 scopus 로고    scopus 로고
    • Silencing disease genes in the laboratory and the clinic
    • [4] Watts, J.K., Corey, D.R., Silencing disease genes in the laboratory and the clinic. J. Pathol. 226 (2012), 365–379, 10.1002/path.2993.
    • (2012) J. Pathol. , vol.226 , pp. 365-379
    • Watts, J.K.1    Corey, D.R.2
  • 5
    • 77956901498 scopus 로고    scopus 로고
    • The promise of microRNA replacement therapy
    • [5] Bader, A.G., Brown, D., Winkler, M., The promise of microRNA replacement therapy. Cancer Res. 70 (2010), 7027–7030, 10.1158/0008-5472.CAN-10-2010.
    • (2010) Cancer Res. , vol.70 , pp. 7027-7030
    • Bader, A.G.1    Brown, D.2    Winkler, M.3
  • 6
    • 84939802078 scopus 로고    scopus 로고
    • Oligonucleotide therapies: the past and the present
    • [6] Lundin, K.E., Gissberg, O., Smith, C.I.E., Oligonucleotide therapies: the past and the present. Hum. Gene Ther. 26 (2015), 475–485, 10.1089/hum.2015.070.
    • (2015) Hum. Gene Ther. , vol.26 , pp. 475-485
    • Lundin, K.E.1    Gissberg, O.2    Smith, C.I.E.3
  • 7
    • 84954214717 scopus 로고    scopus 로고
    • Biology and applications of CRISPR systems: harnessing nature's toolbox for genome engineering
    • [7] Wright, A.V., Nuñez, J.K., Doudna, J.A., Biology and applications of CRISPR systems: harnessing nature's toolbox for genome engineering. Cell 164 (2016), 29–44, 10.1016/j.cell.2015.12.035.
    • (2016) Cell , vol.164 , pp. 29-44
    • Wright, A.V.1    Nuñez, J.K.2    Doudna, J.A.3
  • 8
    • 84923106217 scopus 로고    scopus 로고
    • Therapeutic genome editing: prospects and challenges
    • [8] Cox, D.B.T., Platt, R.J., Zhang, F., Therapeutic genome editing: prospects and challenges. Nat. Med. 21 (2015), 121–131, 10.1038/nm.3793.
    • (2015) Nat. Med. , vol.21 , pp. 121-131
    • Cox, D.B.T.1    Platt, R.J.2    Zhang, F.3
  • 9
    • 84923828111 scopus 로고    scopus 로고
    • Synthetic chemically modified mRNA (modRNA): toward a new technology platform for cardiovascular biology and medicine
    • [9] Chien, K.R., Zangi, L., Lui, K.O., Synthetic chemically modified mRNA (modRNA): toward a new technology platform for cardiovascular biology and medicine. Cold Spring Harb. Perspect. Med., 5, 2015, a014035, 10.1101/cshperspect.a014035.
    • (2015) Cold Spring Harb. Perspect. Med. , vol.5 , pp. a014035
    • Chien, K.R.1    Zangi, L.2    Lui, K.O.3
  • 10
    • 84937252963 scopus 로고    scopus 로고
    • Pharmacokinetics, biodistribution and cell uptake of antisense oligonucleotides
    • [10] Geary, R.S., Norris, D., Yu, R., Bennett, C.F., Pharmacokinetics, biodistribution and cell uptake of antisense oligonucleotides. Adv. Drug Deliv. Rev., 2015, 10.1016/j.addr.2015.01.008.
    • (2015) Adv. Drug Deliv. Rev.
    • Geary, R.S.1    Norris, D.2    Yu, R.3    Bennett, C.F.4
  • 11
    • 84896911109 scopus 로고    scopus 로고
    • Cellular uptake and intracellular trafficking of oligonucleotides: implications for oligonucleotide pharmacology
    • [11] Juliano, R.l., Ming, X., Carver, K., Laing, B., Cellular uptake and intracellular trafficking of oligonucleotides: implications for oligonucleotide pharmacology. Nucleic Acid Ther. 24 (2014), 101–113, 10.1089/nat.2013.0463.
    • (2014) Nucleic Acid Ther. , vol.24 , pp. 101-113
    • Juliano, R.L.1    Ming, X.2    Carver, K.3    Laing, B.4
  • 12
    • 84944339068 scopus 로고    scopus 로고
    • Gene therapy returns to centre stage
    • [12] Naldini, L., Gene therapy returns to centre stage. Nature 526 (2015), 351–360, 10.1038/nature15818.
    • (2015) Nature , vol.526 , pp. 351-360
    • Naldini, L.1
  • 14
    • 84942046481 scopus 로고    scopus 로고
    • Nucleic acid therapeutics using polyplexes: a journey of 50 years (and beyond)
    • [14] Lächelt, U., Wagner, E., Nucleic acid therapeutics using polyplexes: a journey of 50 years (and beyond). Chem. Rev. 115 (2015), 11043–11078, 10.1021/cr5006793.
    • (2015) Chem. Rev. , vol.115 , pp. 11043-11078
    • Lächelt, U.1    Wagner, E.2
  • 15
    • 84920078224 scopus 로고    scopus 로고
    • Sequence-defined polymers for the delivery of oligonucleotides
    • [15] Lehto, T., Wagner, E., Sequence-defined polymers for the delivery of oligonucleotides. Nanomedicine 9 (2014), 2843–2859, 10.2217/nnm.14.166.
    • (2014) Nanomedicine , vol.9 , pp. 2843-2859
    • Lehto, T.1    Wagner, E.2
  • 16
    • 84955137316 scopus 로고    scopus 로고
    • Classes of cell-penetrating peptides
    • [16] Pooga, M., Langel, Ü., Classes of cell-penetrating peptides. Methods Mol. Biol. Clifton N.J. 1324 (2015), 3–28, 10.1007/978-1-4939-2806-4_1.
    • (2015) Methods Mol. Biol. Clifton N.J. , vol.1324 , pp. 3-28
    • Pooga, M.1    Langel, Ü.2
  • 17
    • 68549110328 scopus 로고    scopus 로고
    • Twenty years of cell-penetrating peptides: from molecular mechanisms to therapeutics
    • [17] Heitz, F., Morris, M.C., Divita, G., Twenty years of cell-penetrating peptides: from molecular mechanisms to therapeutics. Br. J. Pharmacol. 157 (2009), 195–206, 10.1111/j.1476-5381.2009.00057.x.
    • (2009) Br. J. Pharmacol. , vol.157 , pp. 195-206
    • Heitz, F.1    Morris, M.C.2    Divita, G.3
  • 18
    • 84878668366 scopus 로고    scopus 로고
    • Arginine-rich peptides: methods of translocation through biological membranes
    • [18] Futaki, S., Hirose, H., Nakase, I., Arginine-rich peptides: methods of translocation through biological membranes. Curr. Pharm. Des. 19 (2013), 2863–2868.
    • (2013) Curr. Pharm. Des. , vol.19 , pp. 2863-2868
    • Futaki, S.1    Hirose, H.2    Nakase, I.3
  • 19
    • 84862734920 scopus 로고    scopus 로고
    • Cell-penetrating peptides for the delivery of nucleic acids
    • [19] Lehto, T., Kurrikoff, K., Langel, Ü., Cell-penetrating peptides for the delivery of nucleic acids. Expert Opin. Drug Deliv. 9 (2012), 823–836, 10.1517/17425247.2012.689285.
    • (2012) Expert Opin. Drug Deliv. , vol.9 , pp. 823-836
    • Lehto, T.1    Kurrikoff, K.2    Langel, Ü.3
  • 20
    • 84862629948 scopus 로고    scopus 로고
    • Use of cell-penetrating-peptides in oligonucleotide splice switching therapy
    • [20] El Andaloussi, S.A., Hammond, S.M., Mäger, I., Wood, M.J.A., Use of cell-penetrating-peptides in oligonucleotide splice switching therapy. Curr. Gene Ther. 12 (2012), 161–178.
    • (2012) Curr. Gene Ther. , vol.12 , pp. 161-178
    • El Andaloussi, S.A.1    Hammond, S.M.2    Mäger, I.3    Wood, M.J.A.4
  • 22
    • 84875146033 scopus 로고    scopus 로고
    • PTD/CPP peptide-mediated delivery of siRNAs
    • [22] Presente, A., Dowdy, S.F., PTD/CPP peptide-mediated delivery of siRNAs. Curr. Pharm. Des. 19 (2013), 2943–2947.
    • (2013) Curr. Pharm. Des. , vol.19 , pp. 2943-2947
    • Presente, A.1    Dowdy, S.F.2
  • 23
    • 38949213664 scopus 로고    scopus 로고
    • Predicting cell-penetrating peptides
    • [23] Hansen, M., Kilk, K., Langel, U., Predicting cell-penetrating peptides. Adv. Drug Deliv. Rev. 60 (2008), 572–579, 10.1016/j.addr.2007.09.003.
    • (2008) Adv. Drug Deliv. Rev. , vol.60 , pp. 572-579
    • Hansen, M.1    Kilk, K.2    Langel, U.3
  • 24
    • 84900988583 scopus 로고    scopus 로고
    • The uptake of arginine-rich cell-penetrating peptides: putting the puzzle together
    • [24] Brock, R., The uptake of arginine-rich cell-penetrating peptides: putting the puzzle together. Bioconjug. Chem. 25 (2014), 863–868, 10.1021/bc500017t.
    • (2014) Bioconjug. Chem. , vol.25 , pp. 863-868
    • Brock, R.1
  • 25
    • 84881023889 scopus 로고    scopus 로고
    • Insights into cell entry and intracellular trafficking of peptide and protein drugs provided by electron microscopy
    • [25] Margus, H., Padari, K., Pooga, M., Insights into cell entry and intracellular trafficking of peptide and protein drugs provided by electron microscopy. Adv. Drug Deliv. Rev. 65 (2013), 1031–1038, 10.1016/j.addr.2013.04.013.
    • (2013) Adv. Drug Deliv. Rev. , vol.65 , pp. 1031-1038
    • Margus, H.1    Padari, K.2    Pooga, M.3
  • 26
    • 84878638891 scopus 로고    scopus 로고
    • Endocytosis, intracellular traffic and fate of cell penetrating peptide based conjugates and nanoparticles
    • [26] Cleal, K., He, L., Watson, P.D., Jones, A.T., Endocytosis, intracellular traffic and fate of cell penetrating peptide based conjugates and nanoparticles. Curr. Pharm. Des. 19 (2013), 2878–2894.
    • (2013) Curr. Pharm. Des. , vol.19 , pp. 2878-2894
    • Cleal, K.1    He, L.2    Watson, P.D.3    Jones, A.T.4
  • 27
    • 84878526418 scopus 로고    scopus 로고
    • Endocytosis of gene delivery vectors: from clathrin-dependent to lipid raft-mediated endocytosis
    • [27] El-Sayed, A., Harashima, H., Endocytosis of gene delivery vectors: from clathrin-dependent to lipid raft-mediated endocytosis. Mol. Ther. 21 (2013), 1118–1130, 10.1038/mt.2013.54.
    • (2013) Mol. Ther. , vol.21 , pp. 1118-1130
    • El-Sayed, A.1    Harashima, H.2
  • 29
    • 65549133368 scopus 로고    scopus 로고
    • Delivery of macromolecules using arginine-rich cell-penetrating peptides: ways to overcome endosomal entrapment
    • [29] El-Sayed, A., Futaki, S., Harashima, H., Delivery of macromolecules using arginine-rich cell-penetrating peptides: ways to overcome endosomal entrapment. AAPS J. 11 (2009), 13–22, 10.1208/s12248-008-9071-2.
    • (2009) AAPS J. , vol.11 , pp. 13-22
    • El-Sayed, A.1    Futaki, S.2    Harashima, H.3
  • 31
    • 84893541929 scopus 로고    scopus 로고
    • A chemical view of oligonucleotides for exon skipping and related drug applications
    • [31] Järver, P., O'Donovan, L., Gait, M.J., A chemical view of oligonucleotides for exon skipping and related drug applications. Nucleic Acid Ther. 24 (2013), 37–47, 10.1089/nat.2013.0454.
    • (2013) Nucleic Acid Ther. , vol.24 , pp. 37-47
    • Järver, P.1    O'Donovan, L.2    Gait, M.J.3
  • 33
    • 38949184554 scopus 로고    scopus 로고
    • Delivery of proteins and nucleic acids using a non-covalent peptide-based strategy
    • [33] Deshayes, S., Morris, M., Heitz, F., Divita, G., Delivery of proteins and nucleic acids using a non-covalent peptide-based strategy. Adv. Drug Deliv. Rev. 60 (2008), 537–547, 10.1016/j.addr.2007.09.005.
    • (2008) Adv. Drug Deliv. Rev. , vol.60 , pp. 537-547
    • Deshayes, S.1    Morris, M.2    Heitz, F.3    Divita, G.4
  • 34
    • 81255166873 scopus 로고    scopus 로고
    • Peptide nanoparticles for oligonucleotide delivery
    • [34] Lehto, T., Ezzat, K., Langel, U., Peptide nanoparticles for oligonucleotide delivery. Prog. Mol. Biol. Transl. Sci. 104 (2011), 397–426, 10.1016/B978-0-12-416020-0.00010-3.
    • (2011) Prog. Mol. Biol. Transl. Sci. , vol.104 , pp. 397-426
    • Lehto, T.1    Ezzat, K.2    Langel, U.3
  • 35
    • 0026341239 scopus 로고
    • Sequence-selective recognition of DNA by strand displacement with a thymine-substituted polyamide
    • [35] Nielsen, P.E., Egholm, M., Berg, R.H., Buchardt, O., Sequence-selective recognition of DNA by strand displacement with a thymine-substituted polyamide. Science 254 (1991), 1497–1500, 10.1126/science.1962210.
    • (1991) Science , vol.254 , pp. 1497-1500
    • Nielsen, P.E.1    Egholm, M.2    Berg, R.H.3    Buchardt, O.4
  • 37
    • 33646950391 scopus 로고    scopus 로고
    • Evaluation of cell-penetrating peptides (CPPs) as vehicles for intracellular delivery of antisense peptide nucleic acid (PNA)
    • [37] Bendifallah, N., Rasmussen, F.W., Zachar, V., Ebbesen, P., Nielsen, P.E., Koppelhus, U., Evaluation of cell-penetrating peptides (CPPs) as vehicles for intracellular delivery of antisense peptide nucleic acid (PNA). Bioconjug. Chem. 17 (2006), 750–758, 10.1021/bc050283q.
    • (2006) Bioconjug. Chem. , vol.17 , pp. 750-758
    • Bendifallah, N.1    Rasmussen, F.W.2    Zachar, V.3    Ebbesen, P.4    Nielsen, P.E.5    Koppelhus, U.6
  • 39
    • 34548183128 scopus 로고    scopus 로고
    • Assessing the delivery efficacy and internalization route of cell-penetrating peptides
    • [39] El Andaloussi, S., Guterstam, P., Langel, U., Assessing the delivery efficacy and internalization route of cell-penetrating peptides. Nat. Protoc. 2 (2007), 2043–2047, 10.1038/nprot.2007.302.
    • (2007) Nat. Protoc. , vol.2 , pp. 2043-2047
    • El Andaloussi, S.1    Guterstam, P.2    Langel, U.3
  • 41
    • 84856964238 scopus 로고    scopus 로고
    • Targeted gene modification of hematopoietic progenitor cells in mice following systemic administration of a PNA-peptide conjugate
    • [41] Rogers, F.A., Lin, S.S., Hegan, D.C., Krause, D.S., Glazer, P.M., Targeted gene modification of hematopoietic progenitor cells in mice following systemic administration of a PNA-peptide conjugate. Mol. Ther. J. Am. Soc. Gene Ther. 20 (2012), 109–118, 10.1038/mt.2011.163.
    • (2012) Mol. Ther. J. Am. Soc. Gene Ther. , vol.20 , pp. 109-118
    • Rogers, F.A.1    Lin, S.S.2    Hegan, D.C.3    Krause, D.S.4    Glazer, P.M.5
  • 44
    • 33847036106 scopus 로고    scopus 로고
    • Vectorization of morpholino oligomers by the (R-Ahx-R)4 peptide allows efficient splicing correction in the absence of endosomolytic agents
    • [44] Abes, S., Moulton, H.M., Clair, P., Prevot, P., Youngblood, D.S., Wu, R.P., Iversen, P.L., Lebleu, B., Vectorization of morpholino oligomers by the (R-Ahx-R)4 peptide allows efficient splicing correction in the absence of endosomolytic agents. J. Control. Release 116 (2006), 304–313, 10.1016/j.jconrel.2006.09.011.
    • (2006) J. Control. Release , vol.116 , pp. 304-313
    • Abes, S.1    Moulton, H.M.2    Clair, P.3    Prevot, P.4    Youngblood, D.S.5    Wu, R.P.6    Iversen, P.L.7    Lebleu, B.8
  • 46
    • 0037276860 scopus 로고    scopus 로고
    • The heart in human dystrophinopathies
    • (doi:68446)
    • [46] Finsterer, J., Stöllberger, C., The heart in human dystrophinopathies. Cardiology 99 (2003), 1–19 (doi:68446).
    • (2003) Cardiology , vol.99 , pp. 1-19
    • Finsterer, J.1    Stöllberger, C.2
  • 47
    • 84964561725 scopus 로고    scopus 로고
    • Current understanding of molecular pathology and treatment of cardiomyopathy in duchenne muscular dystrophy
    • [47] van Westering, T.L.E., Betts, C.A., Wood, M.J.A., Current understanding of molecular pathology and treatment of cardiomyopathy in duchenne muscular dystrophy. Mol. Basel Switz. 20 (2015), 8823–8855, 10.3390/molecules20058823.
    • (2015) Mol. Basel Switz. , vol.20 , pp. 8823-8855
    • van Westering, T.L.E.1    Betts, C.A.2    Wood, M.J.A.3
  • 48
    • 84878684143 scopus 로고    scopus 로고
    • Splicing therapy for neuromuscular disease
    • [48] Douglas, A.G.L., Wood, M.J.A., Splicing therapy for neuromuscular disease. Mol. Cell. Neurosci. 56 (2013), 169–185, 10.1016/j.mcn.2013.04.005.
    • (2013) Mol. Cell. Neurosci. , vol.56 , pp. 169-185
    • Douglas, A.G.L.1    Wood, M.J.A.2
  • 49
    • 84877872340 scopus 로고    scopus 로고
    • Clinical trials using antisense oligonucleotides in duchenne muscular dystrophy
    • [49] Koo, T., Wood, M.J., Clinical trials using antisense oligonucleotides in duchenne muscular dystrophy. Hum. Gene Ther. 24 (2013), 479–488, 10.1089/hum.2012.234.
    • (2013) Hum. Gene Ther. , vol.24 , pp. 479-488
    • Koo, T.1    Wood, M.J.2
  • 50
    • 57049102809 scopus 로고    scopus 로고
    • Cell-penetrating peptide-conjugated antisense oligonucleotides restore systemic muscle and cardiac dystrophin expression and function
    • [50] Yin, H., Moulton, H.M., Seow, Y., Boyd, C., Boutilier, J., Iverson, P., Wood, M.J., Cell-penetrating peptide-conjugated antisense oligonucleotides restore systemic muscle and cardiac dystrophin expression and function. Hum. Mol. Genet. 17 (2008), 3909–3918, 10.1093/hmg/ddn293.
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 3909-3918
    • Yin, H.1    Moulton, H.M.2    Seow, Y.3    Boyd, C.4    Boutilier, J.5    Iverson, P.6    Wood, M.J.7
  • 52
    • 70350697818 scopus 로고    scopus 로고
    • A fusion peptide directs enhanced systemic dystrophin exon skipping and functional restoration in dystrophin-deficient mdx mice
    • [52] Yin, H., Moulton, H.M., Betts, C., Seow, Y., Boutilier, J., Iverson, P.L., Wood, M.J.A., A fusion peptide directs enhanced systemic dystrophin exon skipping and functional restoration in dystrophin-deficient mdx mice. Hum. Mol. Genet. 18 (2009), 4405–4414, 10.1093/hmg/ddp395.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 4405-4414
    • Yin, H.1    Moulton, H.M.2    Betts, C.3    Seow, Y.4    Boutilier, J.5    Iverson, P.L.6    Wood, M.J.A.7
  • 53
    • 79959995255 scopus 로고    scopus 로고
    • Pip5 transduction peptides direct high efficiency oligonucleotide-mediated dystrophin exon skipping in heart and phenotypic correction in mdx mice
    • [53] Yin, H., Saleh, A.F., Betts, C., Camelliti, P., Seow, Y., Ashraf, S., Arzumanov, A., Hammond, S., Merritt, T., Gait, M.J., Wood, M.J., Pip5 transduction peptides direct high efficiency oligonucleotide-mediated dystrophin exon skipping in heart and phenotypic correction in mdx mice. Mol. Ther. 19 (2011), 1295–1303, 10.1038/mt.2011.79.
    • (2011) Mol. Ther. , vol.19 , pp. 1295-1303
    • Yin, H.1    Saleh, A.F.2    Betts, C.3    Camelliti, P.4    Seow, Y.5    Ashraf, S.6    Arzumanov, A.7    Hammond, S.8    Merritt, T.9    Gait, M.J.10    Wood, M.J.11
  • 54
    • 84868371403 scopus 로고    scopus 로고
    • Pip6-PMO, a new generation of peptide-oligonucleotide conjugates with improved cardiac exon skipping activity for DMD treatment
    • [54] Betts, C., Saleh, A.F., Arzumanov, A.A., Hammond, S.M., Godfrey, C., Coursindel, T., Gait, M.J., Wood, M.J., Pip6-PMO, a new generation of peptide-oligonucleotide conjugates with improved cardiac exon skipping activity for DMD treatment. Mol. Ther.–Nucleic Acids, 1, 2012, e38, 10.1038/mtna.2012.30.
    • (2012) Mol. Ther.–Nucleic Acids , vol.1 , pp. e38
    • Betts, C.1    Saleh, A.F.2    Arzumanov, A.A.3    Hammond, S.M.4    Godfrey, C.5    Coursindel, T.6    Gait, M.J.7    Wood, M.J.8
  • 61
    • 79957445457 scopus 로고    scopus 로고
    • Inhibition of porcine reproductive and respiratory syndrome virus infection in piglets by a peptide-conjugated morpholino oligomer
    • [61] Opriessnig, T., Patel, D., Wang, R., Halbur, P.G., Meng, X.-J., Stein, D.A., Zhang, Y.-J., Inhibition of porcine reproductive and respiratory syndrome virus infection in piglets by a peptide-conjugated morpholino oligomer. Antivir. Res. 91 (2011), 36–42, 10.1016/j.antiviral.2011.04.012.
    • (2011) Antivir. Res. , vol.91 , pp. 36-42
    • Opriessnig, T.1    Patel, D.2    Wang, R.3    Halbur, P.G.4    Meng, X.-J.5    Stein, D.A.6    Zhang, Y.-J.7
  • 63
    • 49649101361 scopus 로고    scopus 로고
    • Treatment of AG129 mice with antisense morpholino oligomers increases survival time following challenge with dengue 2 virus
    • [63] Stein, D.A., Huang, C.Y.-H., Silengo, S., Amantana, A., Crumley, S., Blouch, R.E., Iversen, P.L., Kinney, R.M., Treatment of AG129 mice with antisense morpholino oligomers increases survival time following challenge with dengue 2 virus. J. Antimicrob. Chemother. 62 (2008), 555–565, 10.1093/jac/dkn221.
    • (2008) J. Antimicrob. Chemother. , vol.62 , pp. 555-565
    • Stein, D.A.1    Huang, C.Y.-H.2    Silengo, S.3    Amantana, A.4    Crumley, S.5    Blouch, R.E.6    Iversen, P.L.7    Kinney, R.M.8
  • 65
    • 33845903558 scopus 로고    scopus 로고
    • Antisense peptide-phosphorodiamidate morpholino oligomer conjugate: dose–response in mice infected with Escherichia coli
    • [65] Tilley, L.D., Mellbye, B.L., Puckett, S.E., Iversen, P.L., Geller, B.L., Antisense peptide-phosphorodiamidate morpholino oligomer conjugate: dose–response in mice infected with Escherichia coli. J. Antimicrob. Chemother. 59 (2007), 66–73, 10.1093/jac/dkl444.
    • (2007) J. Antimicrob. Chemother. , vol.59 , pp. 66-73
    • Tilley, L.D.1    Mellbye, B.L.2    Puckett, S.E.3    Iversen, P.L.4    Geller, B.L.5
  • 66
    • 80053623455 scopus 로고    scopus 로고
    • Basic peptide-morpholino oligomer conjugate that is very effective in killing bacteria by gene-specific and nonspecific modes
    • [66] Wesolowski, D., Tae, H.S., Gandotra, N., Llopis, P., Shen, N., Altman, S., Basic peptide-morpholino oligomer conjugate that is very effective in killing bacteria by gene-specific and nonspecific modes. Proc. Natl. Acad. Sci. U. S. A. 108 (2011), 16582–16587, 10.1073/pnas.1112561108.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 16582-16587
    • Wesolowski, D.1    Tae, H.S.2    Gandotra, N.3    Llopis, P.4    Shen, N.5    Altman, S.6
  • 67
    • 84870355586 scopus 로고    scopus 로고
    • Peptide conjugated phosphorodiamidate morpholino oligomers increase survival of mice challenged with Ames Bacillus anthracis
    • [67] Panchal, R.G., Geller, B.L., Mellbye, B., Lane, D., Iversen, P.L., Bavari, S., Peptide conjugated phosphorodiamidate morpholino oligomers increase survival of mice challenged with Ames Bacillus anthracis. Nucleic Acid Ther. 22 (2012), 316–322, 10.1089/nat.2012.0362.
    • (2012) Nucleic Acid Ther. , vol.22 , pp. 316-322
    • Panchal, R.G.1    Geller, B.L.2    Mellbye, B.3    Lane, D.4    Iversen, P.L.5    Bavari, S.6
  • 69
    • 0030804766 scopus 로고    scopus 로고
    • A new peptide vector for efficient delivery of oligonucleotides into mammalian cells
    • [69] Morris, M.C., Vidal, P., Chaloin, L., Heitz, F., Divita, G., A new peptide vector for efficient delivery of oligonucleotides into mammalian cells. Nucleic Acids Res. 25 (1997), 2730–2736.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 2730-2736
    • Morris, M.C.1    Vidal, P.2    Chaloin, L.3    Heitz, F.4    Divita, G.5
  • 70
    • 0030890748 scopus 로고    scopus 로고
    • Design, synthesis, and characterization of a cationic peptide that binds to nucleic acids and permeabilizes bilayers
    • [70] Wyman, T.B., Nicol, F., Zelphati, O., Scaria, P.V., Plank, C., Szoka, F.C., Design, synthesis, and characterization of a cationic peptide that binds to nucleic acids and permeabilizes bilayers. Biochemistry (Mosc) 36 (1997), 3008–3017, 10.1021/bi9618474.
    • (1997) Biochemistry (Mosc) , vol.36 , pp. 3008-3017
    • Wyman, T.B.1    Nicol, F.2    Zelphati, O.3    Scaria, P.V.4    Plank, C.5    Szoka, F.C.6
  • 71
    • 0033199787 scopus 로고    scopus 로고
    • A novel potent strategy for gene delivery using a single peptide vector as a carrier
    • [71] Morris, M.C., Chaloin, L., Méry, J., Heitz, F., Divita, G., A novel potent strategy for gene delivery using a single peptide vector as a carrier. Nucleic Acids Res. 27 (1999), 3510–3517.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 3510-3517
    • Morris, M.C.1    Chaloin, L.2    Méry, J.3    Heitz, F.4    Divita, G.5
  • 74
    • 77952580991 scopus 로고    scopus 로고
    • Secondary structure of cell-penetrating peptides controls membrane interaction and insertion
    • [74] Eiríksdóttir, E., Konate, K., Langel, Ü., Divita, G., Deshayes, S., Secondary structure of cell-penetrating peptides controls membrane interaction and insertion. Biochim. Biophys. Acta Biomembr. 1798 (2010), 1119–1128, 10.1016/j.bbamem.2010.03.005.
    • (2010) Biochim. Biophys. Acta Biomembr. , vol.1798 , pp. 1119-1128
    • Eiríksdóttir, E.1    Konate, K.2    Langel, Ü.3    Divita, G.4    Deshayes, S.5
  • 75
    • 79958086652 scopus 로고    scopus 로고
    • Synthesis of all-hydrocarbon stapled α-helical peptides by ring-closing olefin metathesis
    • [75] Kim, Y.-W., Grossmann, T.N., Verdine, G.L., Synthesis of all-hydrocarbon stapled α-helical peptides by ring-closing olefin metathesis. Nat. Protoc. 6 (2011), 761–771, 10.1038/nprot.2011.324.
    • (2011) Nat. Protoc. , vol.6 , pp. 761-771
    • Kim, Y.-W.1    Grossmann, T.N.2    Verdine, G.L.3
  • 77
    • 84909998203 scopus 로고    scopus 로고
    • Chapter six – multifunctional enveloped nanodevices (MENDs)
    • Leaf Huang Dexi Liu Ernst Wagner Academic Press (accessed February 23, 2016)
    • [77] Sato, Y., Nakamura, T., Yamada, Y., Akita, H., Harashima, H., Chapter six – multifunctional enveloped nanodevices (MENDs). Huang, Leaf, Liu, Dexi, Wagner, Ernst, (eds.) Adv. Genet., 2014, Academic Press, 139–204 http://www.sciencedirect.com/science/article/pii/B9780128001486000067 (accessed February 23, 2016).
    • (2014) Adv. Genet. , pp. 139-204
    • Sato, Y.1    Nakamura, T.2    Yamada, Y.3    Akita, H.4    Harashima, H.5
  • 82
    • 84864700457 scopus 로고    scopus 로고
    • Solid formulation of cell-penetrating peptide nanocomplexes with siRNA and their stability in simulated gastric conditions
    • [82] Ezzat, K., Zaghloul, E.M., El Andaloussi, S., Lehto, T., El-Sayed, R., Magdy, T., Smith, C.I., Langel, U., Solid formulation of cell-penetrating peptide nanocomplexes with siRNA and their stability in simulated gastric conditions. J. Control. Release 162 (2012), 1–8, 10.1016/j.jconrel.2012.06.006.
    • (2012) J. Control. Release , vol.162 , pp. 1-8
    • Ezzat, K.1    Zaghloul, E.M.2    El Andaloussi, S.3    Lehto, T.4    El-Sayed, R.5    Magdy, T.6    Smith, C.I.7    Langel, U.8
  • 85
    • 67149093390 scopus 로고    scopus 로고
    • Efficient siRNA delivery into primary cells by a peptide transduction domain-dsRNA binding domain fusion protein
    • [85] Eguchi, A., Meade, B.R., Chang, Y.C., Fredrickson, C.T., Willert, K., Puri, N., Dowdy, S.F., Efficient siRNA delivery into primary cells by a peptide transduction domain-dsRNA binding domain fusion protein. Nat. Biotechnol. 27 (2009), 567–571, 10.1038/nbt.1541.
    • (2009) Nat. Biotechnol. , vol.27 , pp. 567-571
    • Eguchi, A.1    Meade, B.R.2    Chang, Y.C.3    Fredrickson, C.T.4    Willert, K.5    Puri, N.6    Dowdy, S.F.7
  • 86
    • 73949121242 scopus 로고    scopus 로고
    • Induction of in vivo synthetic lethal RNAi responses to treat glioblastoma
    • [86] Michiue, H., Eguchi, A., Scadeng, M., Dowdy, S.F., Induction of in vivo synthetic lethal RNAi responses to treat glioblastoma. Cancer Biol. Ther. 8 (2009), 2306–2313.
    • (2009) Cancer Biol. Ther. , vol.8 , pp. 2306-2313
    • Michiue, H.1    Eguchi, A.2    Scadeng, M.3    Dowdy, S.F.4
  • 91
  • 92
    • 0030904245 scopus 로고    scopus 로고
    • A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus
    • [92] Vivès, E., Brodin, P., Lebleu, B., A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus. J. Biol. Chem. 272 (1997), 16010–16017.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16010-16017
    • Vivès, E.1    Brodin, P.2    Lebleu, B.3
  • 93
    • 0028239908 scopus 로고
    • The third helix of the Antennapedia homeodomain translocates through biological membranes
    • [93] Derossi, D., Joliot, A.H., Chassaing, G., Prochiantz, A., The third helix of the Antennapedia homeodomain translocates through biological membranes. J. Biol. Chem. 269 (1994), 10444–10450.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10444-10450
    • Derossi, D.1    Joliot, A.H.2    Chassaing, G.3    Prochiantz, A.4
  • 94
    • 0029982569 scopus 로고    scopus 로고
    • Cell internalization of the third helix of the Antennapedia homeodomain is receptor-independent
    • [94] Derossi, D., Calvet, S., Trembleau, A., Brunissen, A., Chassaing, G., Prochiantz, A., Cell internalization of the third helix of the Antennapedia homeodomain is receptor-independent. J. Biol. Chem. 271 (1996), 18188–18193.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18188-18193
    • Derossi, D.1    Calvet, S.2    Trembleau, A.3    Brunissen, A.4    Chassaing, G.5    Prochiantz, A.6
  • 95
    • 0032443219 scopus 로고    scopus 로고
    • Mode of action of linear amphipathic alpha-helical antimicrobial peptides
    • [95] Oren, Z., Shai, Y., Mode of action of linear amphipathic alpha-helical antimicrobial peptides. Biopolymers 47 (1998), 451–463, 10.1002/(SICI)1097-0282(1998)47:6<451::AID-BIP4>3.0.CO;2-F.
    • (1998) Biopolymers , vol.47 , pp. 451-463
    • Oren, Z.1    Shai, Y.2
  • 96
    • 79956025776 scopus 로고    scopus 로고
    • Antimicrobial peptides with cell-penetrating peptide properties and vice versa
    • [96] Splith, K., Neundorf, I., Antimicrobial peptides with cell-penetrating peptide properties and vice versa. Eur. Biophys. J. EBJ 40 (2011), 387–397, 10.1007/s00249-011-0682-7.
    • (2011) Eur. Biophys. J. EBJ , vol.40 , pp. 387-397
    • Splith, K.1    Neundorf, I.2
  • 97
    • 33749385780 scopus 로고    scopus 로고
    • Cell-penetrating peptides and antimicrobial peptides: how different are they?
    • [97] Henriques, S.T., Melo, M.N., Castanho, M.A.R.B., Cell-penetrating peptides and antimicrobial peptides: how different are they?. Biochem. J. 399 (2006), 1–7, 10.1042/BJ20061100.
    • (2006) Biochem. J. , vol.399 , pp. 1-7
    • Henriques, S.T.1    Melo, M.N.2    Castanho, M.A.R.B.3
  • 99
    • 1642578411 scopus 로고    scopus 로고
    • Mechanism of improved gene transfer by the N-terminal stearylation of octaarginine: enhanced cellular association by hydrophobic core formation
    • [99] Khalil, I.A., Futaki, S., Niwa, M., Baba, Y., Kaji, N., Kamiya, H., Harashima, H., Mechanism of improved gene transfer by the N-terminal stearylation of octaarginine: enhanced cellular association by hydrophobic core formation. Gene Ther. 11 (2004), 636–644, 10.1038/sj.gt.3302128.
    • (2004) Gene Ther. , vol.11 , pp. 636-644
    • Khalil, I.A.1    Futaki, S.2    Niwa, M.3    Baba, Y.4    Kaji, N.5    Kamiya, H.6    Harashima, H.7
  • 101
    • 67651211690 scopus 로고    scopus 로고
    • Enhanced gene expression by a novel stearylated INF7 peptide derivative through fusion independent endosomal escape
    • [101] El-Sayed, A., Masuda, T., Khalil, I., Akita, H., Harashima, H., Enhanced gene expression by a novel stearylated INF7 peptide derivative through fusion independent endosomal escape. J. Control. Release Off. J. Control. Release Soc. 138 (2009), 160–167, 10.1016/j.jconrel.2009.05.018.
    • (2009) J. Control. Release Off. J. Control. Release Soc. , vol.138 , pp. 160-167
    • El-Sayed, A.1    Masuda, T.2    Khalil, I.3    Akita, H.4    Harashima, H.5
  • 102
  • 103
    • 77957017688 scopus 로고    scopus 로고
    • Cationic cell-penetrating peptides induce ceramide formation via acid sphingomyelinase: implications for uptake
    • [103] Verdurmen, W.P.R., Thanos, M., Ruttekolk, I.R., Gulbins, E., Brock, R., Cationic cell-penetrating peptides induce ceramide formation via acid sphingomyelinase: implications for uptake. J. Control. Release Off. J. Control. Release Soc. 147 (2010), 171–179, 10.1016/j.jconrel.2010.06.030.
    • (2010) J. Control. Release Off. J. Control. Release Soc. , vol.147 , pp. 171-179
    • Verdurmen, W.P.R.1    Thanos, M.2    Ruttekolk, I.R.3    Gulbins, E.4    Brock, R.5
  • 104
    • 0035793619 scopus 로고    scopus 로고
    • Internalization of HIV-1 tat requires cell surface heparan sulfate proteoglycans
    • [104] Tyagi, M., Rusnati, M., Presta, M., Giacca, M., Internalization of HIV-1 tat requires cell surface heparan sulfate proteoglycans. J. Biol. Chem. 276 (2001), 3254–3261, 10.1074/jbc.M006701200.
    • (2001) J. Biol. Chem. , vol.276 , pp. 3254-3261
    • Tyagi, M.1    Rusnati, M.2    Presta, M.3    Giacca, M.4
  • 105
    • 0037119348 scopus 로고    scopus 로고
    • Efficiency of protein transduction is cell type-dependent and is enhanced by dextran sulfate
    • [105] Mai, J.C., Shen, H., Watkins, S.C., Cheng, T., Robbins, P.D., Efficiency of protein transduction is cell type-dependent and is enhanced by dextran sulfate. J. Biol. Chem. 277 (2002), 30208–30218, 10.1074/jbc.M204202200.
    • (2002) J. Biol. Chem. , vol.277 , pp. 30208-30218
    • Mai, J.C.1    Shen, H.2    Watkins, S.C.3    Cheng, T.4    Robbins, P.D.5
  • 106
    • 0037333830 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycan as a plasma membrane carrier
    • [106] Belting, M., Heparan sulfate proteoglycan as a plasma membrane carrier. Trends Biochem. Sci. 28 (2003), 145–151, 10.1016/S0968-0004(03)00031-8.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 145-151
    • Belting, M.1
  • 107
    • 34548162679 scopus 로고    scopus 로고
    • Cell-surface proteoglycans as molecular portals for cationic peptide and polymer entry into cells
    • [107] Poon, G.M.K., Gariépy, J., Cell-surface proteoglycans as molecular portals for cationic peptide and polymer entry into cells. Biochem. Soc. Trans. 35 (2007), 788–793, 10.1042/BST0350788.
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 788-793
    • Poon, G.M.K.1    Gariépy, J.2
  • 110
    • 84883158032 scopus 로고    scopus 로고
    • Scavenger receptors in homeostasis and immunity
    • [110] Canton, J., Neculai, D., Grinstein, S., Scavenger receptors in homeostasis and immunity. Nat. Rev. Immunol. 13 (2013), 621–634, 10.1038/nri3515.
    • (2013) Nat. Rev. Immunol. , vol.13 , pp. 621-634
    • Canton, J.1    Neculai, D.2    Grinstein, S.3
  • 111
    • 0034529953 scopus 로고    scopus 로고
    • Uptake of HIV-1 tat protein mediated by low-density lipoprotein receptor-related protein disrupts the neuronal metabolic balance of the receptor ligands
    • [111] Liu, Y., Jones, M., Hingtgen, C.M., Bu, G., Laribee, N., Tanzi, R.E., Moir, R.D., Nath, A., He, J.J., Uptake of HIV-1 tat protein mediated by low-density lipoprotein receptor-related protein disrupts the neuronal metabolic balance of the receptor ligands. Nat. Med. 6 (2000), 1380–1387, 10.1038/82199.
    • (2000) Nat. Med. , vol.6 , pp. 1380-1387
    • Liu, Y.1    Jones, M.2    Hingtgen, C.M.3    Bu, G.4    Laribee, N.5    Tanzi, R.E.6    Moir, R.D.7    Nath, A.8    He, J.J.9
  • 114
    • 84955264852 scopus 로고    scopus 로고
    • Role of scavenger receptors in peptide-based delivery of plasmid DNA across a blood–brain barrier model
    • [114] Srimanee, A., Regberg, J., Hällbrink, M., Vajragupta, O., Langel, Ü., Role of scavenger receptors in peptide-based delivery of plasmid DNA across a blood–brain barrier model. Int. J. Pharm. 500 (2016), 128–135, 10.1016/j.ijpharm.2016.01.014.
    • (2016) Int. J. Pharm. , vol.500 , pp. 128-135
    • Srimanee, A.1    Regberg, J.2    Hällbrink, M.3    Vajragupta, O.4    Langel, Ü.5
  • 116
    • 84911474070 scopus 로고    scopus 로고
    • The membrane-lytic peptides K8 L9 and melittin enter cancer cells via receptor endocytosis following subcytotoxic exposure
    • [116] Kohno, M., Horibe, T., Ohara, K., Ito, S., Kawakami, K., The membrane-lytic peptides K8 L9 and melittin enter cancer cells via receptor endocytosis following subcytotoxic exposure. Chem. Biol. 21 (2014), 1522–1532, 10.1016/j.chembiol.2014.09.008.
    • (2014) Chem. Biol. , vol.21 , pp. 1522-1532
    • Kohno, M.1    Horibe, T.2    Ohara, K.3    Ito, S.4    Kawakami, K.5
  • 118
    • 84937252943 scopus 로고    scopus 로고
    • Cellular antisense activity of PNA-Oligo(bicycloguanidinium) conjugates forming self-assembled nanoaggregates
    • [118] Valero, J., Shiraishi, T., de Mendoza, J., Nielsen, P.E., Cellular antisense activity of PNA-Oligo(bicycloguanidinium) conjugates forming self-assembled nanoaggregates. Chembiochem Eur. J. Chem. Biol. 16 (2015), 1593–1600, 10.1002/cbic.201500172.
    • (2015) Chembiochem Eur. J. Chem. Biol. , vol.16 , pp. 1593-1600
    • Valero, J.1    Shiraishi, T.2    de Mendoza, J.3    Nielsen, P.E.4
  • 119
    • 22144477899 scopus 로고    scopus 로고
    • Mechanics of receptor-mediated endocytosis
    • [119] Gao, H., Shi, W., Freund, L.B., Mechanics of receptor-mediated endocytosis. Proc. Natl. Acad. Sci. U. S. A. 102 (2005), 9469–9474, 10.1073/pnas.0503879102.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 9469-9474
    • Gao, H.1    Shi, W.2    Freund, L.B.3
  • 120
    • 58149213996 scopus 로고    scopus 로고
    • Size and shape effects on diffusion and absorption of colloidal particles near a partially absorbing sphere: implications for uptake of nanoparticles in animal cells
    • [120] Shi, W., Wang, J., Fan, X., Gao, H., Size and shape effects on diffusion and absorption of colloidal particles near a partially absorbing sphere: implications for uptake of nanoparticles in animal cells. Phys. Rev. E Stat. Nonlinear Soft Matter Phys., 78, 2008, 061914, 10.1103/PhysRevE.78.061914.
    • (2008) Phys. Rev. E Stat. Nonlinear Soft Matter Phys. , vol.78 , pp. 061914
    • Shi, W.1    Wang, J.2    Fan, X.3    Gao, H.4
  • 121
    • 25144520907 scopus 로고    scopus 로고
    • On the mechanisms of the internalization of S4(13)-PV cell-penetrating peptide
    • [121] Mano, M., Teodósio, C., Paiva, A., Simões, S., Pedroso de Lima, M.C., On the mechanisms of the internalization of S4(13)-PV cell-penetrating peptide. Biochem. J. 390 (2005), 603–612, 10.1042/BJ20050577.
    • (2005) Biochem. J. , vol.390 , pp. 603-612
    • Mano, M.1    Teodósio, C.2    Paiva, A.3    Simões, S.4    Pedroso de Lima, M.C.5
  • 122
    • 77951285705 scopus 로고    scopus 로고
    • S4(13)-PV cell-penetrating peptide forms nanoparticle-like structures to gain entry into cells
    • [122] Padari, K., Koppel, K., Lorents, A., Hällbrink, M., Mano, M., Pedroso de Lima, M.C., Pooga, M., S4(13)-PV cell-penetrating peptide forms nanoparticle-like structures to gain entry into cells. Bioconjug. Chem. 21 (2010), 774–783, 10.1021/bc900577e.
    • (2010) Bioconjug. Chem. , vol.21 , pp. 774-783
    • Padari, K.1    Koppel, K.2    Lorents, A.3    Hällbrink, M.4    Mano, M.5    Pedroso de Lima, M.C.6    Pooga, M.7


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