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Volumn 1838, Issue 7, 2014, Pages 1911-1920

Design of novel cell penetrating peptides for the delivery of trehalose into mammalian cells

Author keywords

Cell penetrating peptide; Lyophilization; Mammalian cell; Stabilization; Trehalose

Indexed keywords

CELL PENETRATING PEPTIDE; LYSYLARGINYLLYSYLARGINYLTRYPTOPHANYLHISTIDYLTRYPTOPHAN; TREHALOSE; UNCLASSIFIED DRUG;

EID: 84898759691     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2014.02.011     Document Type: Article
Times cited : (26)

References (51)
  • 1
    • 0030088114 scopus 로고    scopus 로고
    • Long-term storage of tissues by cryopreservation: Critical issues
    • J.O. Karlsson, and M. Toner Long-term storage of tissues by cryopreservation: critical issues Biomaterials 17 1996 243 256
    • (1996) Biomaterials , vol.17 , pp. 243-256
    • Karlsson, J.O.1    Toner, M.2
  • 2
    • 0036188792 scopus 로고    scopus 로고
    • The trehalose myth revisited: Introduction to a symposium on stabilization of cells in the dry state
    • J.H. Crowe, L.M. Crowe, A.E. Oliver, N. Tsvetkova, W. Wolkers, and F. Tablin The trehalose myth revisited: introduction to a symposium on stabilization of cells in the dry state Cryobiology 43 2001 89 105
    • (2001) Cryobiology , vol.43 , pp. 89-105
    • Crowe, J.H.1    Crowe, L.M.2    Oliver, A.E.3    Tsvetkova, N.4    Wolkers, W.5    Tablin, F.6
  • 3
    • 0344025281 scopus 로고
    • Freezing of living cells: Mechanisms and implications
    • P. Mazur Freezing of living cells: mechanisms and implications Am. J. Physiol. 247 1984 C125 C142
    • (1984) Am. J. Physiol. , vol.247
    • Mazur, P.1
  • 5
    • 0033770659 scopus 로고    scopus 로고
    • Stabilization and preservation of Lactobacillus acidophilus in saccharide matrices
    • P.B. Conrad, D.P. Miller, P.R. Cielenski, and J.J. de Pablo Stabilization and preservation of Lactobacillus acidophilus in saccharide matrices Cryobiology 41 2000 17 24
    • (2000) Cryobiology , vol.41 , pp. 17-24
    • Conrad, P.B.1    Miller, D.P.2    Cielenski, P.R.3    De Pablo, J.J.4
  • 6
    • 0032126268 scopus 로고    scopus 로고
    • Stabilization of active recombinant retroviruses in an amorphous dry state with trehalose
    • R.M. Bieganski, A. Fowler, J.R. Morgan, and M. Toner Stabilization of active recombinant retroviruses in an amorphous dry state with trehalose Biotechnol. Prog. 14 1998 615 620
    • (1998) Biotechnol. Prog. , vol.14 , pp. 615-620
    • Bieganski, R.M.1    Fowler, A.2    Morgan, J.R.3    Toner, M.4
  • 9
    • 0032039542 scopus 로고    scopus 로고
    • Multiple effects of trehalose on protein folding in vitro and in vivo
    • M.A. Singer, and S. Lindquist Multiple effects of trehalose on protein folding in vitro and in vivo Mol. Cell 1 1998 639 648
    • (1998) Mol. Cell , vol.1 , pp. 639-648
    • Singer, M.A.1    Lindquist, S.2
  • 10
    • 0032697367 scopus 로고    scopus 로고
    • Freezing, drying, and/or vitrification of membrane-solute-water systems
    • J. Wolfe, and G. Bryant Freezing, drying, and/or vitrification of membrane-solute-water systems Cryobiology 39 1999 103 129
    • (1999) Cryobiology , vol.39 , pp. 103-129
    • Wolfe, J.1    Bryant, G.2
  • 11
    • 0036185789 scopus 로고    scopus 로고
    • Beneficial effect of intracellular trehalose on the membrane integrity of dried mammalian cells
    • T. Chen, J.P. Acker, A. Eroglu, S. Cheley, H. Bayley, A. Fowler, and M. Toner Beneficial effect of intracellular trehalose on the membrane integrity of dried mammalian cells Cryobiology 43 2001 168 181
    • (2001) Cryobiology , vol.43 , pp. 168-181
    • Chen, T.1    Acker, J.P.2    Eroglu, A.3    Cheley, S.4    Bayley, H.5    Fowler, A.6    Toner, M.7
  • 13
    • 0013218062 scopus 로고    scopus 로고
    • Survival of desiccated mammalian cells: Beneficial effects of isotonic media
    • J.P. Acker, A. Fowler, B. Lauman, S. Cheley, and M. Toner Survival of desiccated mammalian cells: beneficial effects of isotonic media Cell Preserv. Technol. 1 2002 129 140
    • (2002) Cell Preserv. Technol. , vol.1 , pp. 129-140
    • Acker, J.P.1    Fowler, A.2    Lauman, B.3    Cheley, S.4    Toner, M.5
  • 15
    • 0034964582 scopus 로고    scopus 로고
    • Human platelets loaded with trehalose survive freeze-drying
    • W.F. Wolkers, N.J. Walker, F. Tablin, and J.H. Crowe Human platelets loaded with trehalose survive freeze-drying Cryobiology 42 2001 79 87
    • (2001) Cryobiology , vol.42 , pp. 79-87
    • Wolkers, W.F.1    Walker, N.J.2    Tablin, F.3    Crowe, J.H.4
  • 16
    • 0347360092 scopus 로고    scopus 로고
    • Loading human mesenchymal stem cells with trehalose by fluid-phase endocytosis
    • A.E. Oliver, K. Jamil, J.H. Crowe, and F. Tablin Loading human mesenchymal stem cells with trehalose by fluid-phase endocytosis Cell Preserv. Technol. 2 2004 35 49
    • (2004) Cell Preserv. Technol. , vol.2 , pp. 35-49
    • Oliver, A.E.1    Jamil, K.2    Crowe, J.H.3    Tablin, F.4
  • 17
  • 18
    • 0037600638 scopus 로고    scopus 로고
    • Peptide-mediated cellular delivery of antisense oligonucleotides and their analogues
    • M.J. Gait Peptide-mediated cellular delivery of antisense oligonucleotides and their analogues Cell. Mol. Life Sci. 60 2003 844 853
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 844-853
    • Gait, M.J.1
  • 20
    • 2342595835 scopus 로고    scopus 로고
    • Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis
    • J.S. Wadia, R.V. Stan, and S.F. Dowdy Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis Nat. Med. 10 2004 310 315
    • (2004) Nat. Med. , vol.10 , pp. 310-315
    • Wadia, J.S.1    Stan, R.V.2    Dowdy, S.F.3
  • 21
    • 84869149275 scopus 로고    scopus 로고
    • Cell-penetrating Peptides and Bioactive Cargos
    • Stockholm University Stockholm
    • K. Kilk Cell-penetrating Peptides and Bioactive Cargos Strategies and mechanisms 2004 Stockholm University Stockholm 66
    • (2004) Strategies and Mechanisms , pp. 66
    • Kilk, K.1
  • 23
    • 79960598683 scopus 로고    scopus 로고
    • Design of acid-activated cell penetrating peptide for delivery of active molecules into cancer cells
    • W. Zhang, J. Song, B. Zhang, L. Liu, K. Wang, and R. Wang Design of acid-activated cell penetrating peptide for delivery of active molecules into cancer cells Bioconjug. Chem. 22 2011 1410 1415
    • (2011) Bioconjug. Chem. , vol.22 , pp. 1410-1415
    • Zhang, W.1    Song, J.2    Zhang, B.3    Liu, L.4    Wang, K.5    Wang, R.6
  • 24
    • 38949104405 scopus 로고    scopus 로고
    • Design of a tumor-homing cell-penetrating peptide
    • H. Myrberg, L. Zhang, M. Mae, and U. Langel Design of a tumor-homing cell-penetrating peptide Bioconjug. Chem. 19 2008 70 75
    • (2008) Bioconjug. Chem. , vol.19 , pp. 70-75
    • Myrberg, H.1    Zhang, L.2    Mae, M.3    Langel, U.4
  • 25
    • 7544226311 scopus 로고    scopus 로고
    • PRODRG: A tool for high-throughput crystallography of protein-ligand complexes
    • A.W. Schuttelkopf, and D.M. van Aalten PRODRG: a tool for high-throughput crystallography of protein-ligand complexes Acta Crystallogr. D 60 2004 1355 1363
    • (2004) Acta Crystallogr. D , vol.60 , pp. 1355-1363
    • Schuttelkopf, A.W.1    Van Aalten, D.M.2
  • 26
    • 36449007976 scopus 로고
    • The effect of long-range electrostatic interactions in simulations of macromolecular crystals - A comparison of the Ewald and truncated list methods
    • D.M. York, T.A. Darden, and L.G. Pedersen The effect of long-range electrostatic interactions in simulations of macromolecular crystals - a comparison of the Ewald and truncated list methods J. Chem. Phys. 99 1993 8345 8348
    • (1993) J. Chem. Phys. , vol.99 , pp. 8345-8348
    • York, D.M.1    Darden, T.A.2    Pedersen, L.G.3
  • 29
    • 0037333830 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycan as a plasma membrane carrier
    • M. Belting Heparan sulfate proteoglycan as a plasma membrane carrier Trends Biochem. Sci. 28 2003 145 151
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 145-151
    • Belting, M.1
  • 30
    • 53249092457 scopus 로고    scopus 로고
    • Structure-activity relationship study of the plasma membrane translocating potential of a short peptide from HIV-1 Tat protein
    • E. Vives, C. Granier, P. Prevot, and B. Lebleu Structure-activity relationship study of the plasma membrane translocating potential of a short peptide from HIV-1 Tat protein Lett. Pept. Sci. 4 1997 429 436
    • (1997) Lett. Pept. Sci. , vol.4 , pp. 429-436
    • Vives, E.1    Granier, C.2    Prevot, P.3    Lebleu, B.4
  • 32
    • 0033794501 scopus 로고    scopus 로고
    • Polyarginine enters cells more efficiently than other polycationic homopolymers
    • D.J. Mitchell, D.T. Kim, L. Steinman, C.G. Fathman, and J.B. Rothbard Polyarginine enters cells more efficiently than other polycationic homopolymers J. Pept. Res. 56 2000 318 325
    • (2000) J. Pept. Res. , vol.56 , pp. 318-325
    • Mitchell, D.J.1    Kim, D.T.2    Steinman, L.3    Fathman, C.G.4    Rothbard, J.B.5
  • 33
    • 84875018353 scopus 로고    scopus 로고
    • Static and dynamic interactions between GALK enzyme and known inhibitors: Guidelines to design new drugs for galactosemic patients
    • F. Chiappori, I. Merelli, L. Milanesi, and A. Marabotti Static and dynamic interactions between GALK enzyme and known inhibitors: guidelines to design new drugs for galactosemic patients Eur. J. Med. Chem. 63 2013 423 434
    • (2013) Eur. J. Med. Chem. , vol.63 , pp. 423-434
    • Chiappori, F.1    Merelli, I.2    Milanesi, L.3    Marabotti, A.4
  • 34
    • 13844256698 scopus 로고    scopus 로고
    • Tat peptide-mediated cellular delivery: Back to basics
    • H. Brooks, B. Lebleu, and E. Vives Tat peptide-mediated cellular delivery: back to basics Adv. Drug Deliv. Rev. 57 2005 559 577
    • (2005) Adv. Drug Deliv. Rev. , vol.57 , pp. 559-577
    • Brooks, H.1    Lebleu, B.2    Vives, E.3
  • 36
    • 55949108077 scopus 로고    scopus 로고
    • Molecular mechanism for the effects of trehalose on beta-hairpin folding revealed by molecular dynamics simulation
    • F.F. Liu, X.Y. Dong, and Y. Sun Molecular mechanism for the effects of trehalose on beta-hairpin folding revealed by molecular dynamics simulation J. Mol. Graph. Model. 27 2008 421 429
    • (2008) J. Mol. Graph. Model. , vol.27 , pp. 421-429
    • Liu, F.F.1    Dong, X.Y.2    Sun, Y.3
  • 37
    • 84975279974 scopus 로고    scopus 로고
    • Force fields and molecular dynamics simulations
    • M.A. González Force fields and molecular dynamics simulations Collect. SFN 12 2011 169 200
    • (2011) Collect. SFN , vol.12 , pp. 169-200
    • González, M.A.1
  • 38
    • 18744387415 scopus 로고    scopus 로고
    • Potential energy functions for atomic-level simulations of water and organic and biomolecular systems
    • W.L. Jorgensen, and J. Tirado-Rives Potential energy functions for atomic-level simulations of water and organic and biomolecular systems Proc. Natl. Acad. Sci. U. S. A. 102 2005 6665 6670
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 6665-6670
    • Jorgensen, W.L.1    Tirado-Rives, J.2
  • 39
    • 68549085272 scopus 로고    scopus 로고
    • Molecular insight into the inhibition effect of trehalose on the nucleation and elongation of amyloid beta-peptide oligomers
    • F.F. Liu, L. Ji, X.Y. Dong, and Y. Sun Molecular insight into the inhibition effect of trehalose on the nucleation and elongation of amyloid beta-peptide oligomers J. Phys. Chem. B 113 2009 11320 11329
    • (2009) J. Phys. Chem. B , vol.113 , pp. 11320-11329
    • Liu, F.F.1    Ji, L.2    Dong, X.Y.3    Sun, Y.4
  • 40
    • 4444359475 scopus 로고    scopus 로고
    • Molecular dynamics simulation study of the interaction of trehalose with lipid membranes
    • M.A. Villarreal, S.B. Diaz, E.A. Disalvo, and G.G. Montich Molecular dynamics simulation study of the interaction of trehalose with lipid membranes Langmuir 20 2004 7844 7851
    • (2004) Langmuir , vol.20 , pp. 7844-7851
    • Villarreal, M.A.1    Diaz, S.B.2    Disalvo, E.A.3    Montich, G.G.4
  • 41
    • 80051556888 scopus 로고    scopus 로고
    • Effects of glycosylation on heparin binding and antithrombin activation by heparin
    • L. Pol-Fachin, C.F. Becker, J.A. Guimaraes, and H. Verli Effects of glycosylation on heparin binding and antithrombin activation by heparin Proteins 79 2011 2735 2745
    • (2011) Proteins , vol.79 , pp. 2735-2745
    • Pol-Fachin, L.1    Becker, C.F.2    Guimaraes, J.A.3    Verli, H.4
  • 42
    • 44249097241 scopus 로고    scopus 로고
    • Depiction of the forces participating in the 2-O-sulfo-alpha-l-iduronic acid conformational preference in heparin sequences in aqueous solutions
    • L. Pol-Fachin, and H. Verli Depiction of the forces participating in the 2-O-sulfo-alpha-l-iduronic acid conformational preference in heparin sequences in aqueous solutions Carbohydr. Res. 343 2008 1435 1445
    • (2008) Carbohydr. Res. , vol.343 , pp. 1435-1445
    • Pol-Fachin, L.1    Verli, H.2
  • 43
    • 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
    • E. Vives, P. Brodin, and B. Lebleu 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
    • Vives, E.1    Brodin, P.2    Lebleu, B.3
  • 44
    • 35048856889 scopus 로고    scopus 로고
    • Cargo-dependent cytotoxicity and delivery efficacy of cell-penetrating peptides: A comparative study
    • S. El-Andaloussi, P. Jarver, H.J. Johansson, and U. Langel Cargo-dependent cytotoxicity and delivery efficacy of cell-penetrating peptides: a comparative study Biochem. J. 407 2007 285 292
    • (2007) Biochem. J. , vol.407 , pp. 285-292
    • El-Andaloussi, S.1    Jarver, P.2    Johansson, H.J.3    Langel, U.4
  • 45
    • 0029982569 scopus 로고    scopus 로고
    • Cell internalization of the third helix of the antennapedia homeodomain is receptor-independent
    • D. Derossi, S. Calvet, A. Trembleau, A. Brunissen, G. Chassaing, and A. Prochiantz 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
  • 46
    • 34250835903 scopus 로고    scopus 로고
    • A comprehensive model for the cellular uptake of cationic cell-penetrating peptides
    • F. Duchardt, M. Fotin-Mleczek, H. Schwarz, R. Fischer, and R. Brock A comprehensive model for the cellular uptake of cationic cell-penetrating peptides Traffic 8 2007 848 866
    • (2007) Traffic , vol.8 , pp. 848-866
    • Duchardt, F.1    Fotin-Mleczek, M.2    Schwarz, H.3    Fischer, R.4    Brock, R.5
  • 47
    • 34247093930 scopus 로고    scopus 로고
    • Temperature-, concentration- and cholesterol-dependent translocation of l- and d-octa-arginine across the plasma and nuclear membrane of CD34(+) leukaemia cells
    • M.M. Fretz, N.A. Penning, S. Al-Taei, S. Futaki, T. Takeuchi, I. Nakase, G. Storm, and A.T. Jones Temperature-, concentration- and cholesterol-dependent translocation of l- and d-octa-arginine across the plasma and nuclear membrane of CD34(+) leukaemia cells Biochem. J. 403 2007 335 342
    • (2007) Biochem. J. , vol.403 , pp. 335-342
    • Fretz, M.M.1    Penning, N.A.2    Al-Taei, S.3    Futaki, S.4    Takeuchi, T.5    Nakase, I.6    Storm, G.7    Jones, A.T.8
  • 48
    • 66549123169 scopus 로고    scopus 로고
    • Low concentration thresholds of plasma membranes for rapid energy-independent translocation of a cell-penetrating peptide
    • C.L. Watkins, D. Schmaljohann, S. Futaki, and A.T. Jones Low concentration thresholds of plasma membranes for rapid energy-independent translocation of a cell-penetrating peptide Biochem. J. 420 2009 179 189
    • (2009) Biochem. J. , vol.420 , pp. 179-189
    • Watkins, C.L.1    Schmaljohann, D.2    Futaki, S.3    Jones, A.T.4
  • 50
    • 0034526556 scopus 로고    scopus 로고
    • Liposomes and micelles to target the blood pool for imaging purposes
    • V. Torchilin, J. Babich, and V. Weissig Liposomes and micelles to target the blood pool for imaging purposes J. Liposome Res. 10 2000 483 499
    • (2000) J. Liposome Res. , vol.10 , pp. 483-499
    • Torchilin, V.1    Babich, J.2    Weissig, V.3


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