메뉴 건너뛰기




Volumn 76, Issue 1, 2010, Pages 76-81

Bilayer disruption and liposome restructuring by a homologous series of small Arg-rich synthetic peptides

Author keywords

Domain; Lipid bilayer; Liposome; Peptide; Permeability; Phase behavior

Indexed keywords

1000 MW; BI-LAYER; BREAST CANCER CELLS; CARBOXYFLUORESCEIN; COOPERATIVE EFFECTS; CRYO-TEM; CRYOGENIC TRANSMISSION ELECTRON MICROSCOPY (CRYO-TEM); DIPALMITOYL PHOSPHATIDYLCHOLINE; DOMAIN; ELECTROSTATIC BINDING; HOMOLOGOUS SERIES; LINEAR PEPTIDES; LOW MOLECULAR WEIGHT; MEMBRANE ACTIVITY; MEMBRANE DISRUPTION; PERMEABILIZATION; STRUCTURAL CHANGE; SYNTHETIC PEPTIDE; UNILAMELLAR LIPOSOMES;

EID: 74149084701     PISSN: 09277765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.colsurfb.2009.10.016     Document Type: Article
Times cited : (21)

References (36)
  • 1
    • 34547592118 scopus 로고    scopus 로고
    • Synthesis and evaluation of tripodal peptide analogues for cellular delivery of phosphopeptides
    • Ye G., Nam N.H., Kumar A., Saleh A., Shenoy D.B., Amiji M.M., Lin X., Sun G., and Parang K. Synthesis and evaluation of tripodal peptide analogues for cellular delivery of phosphopeptides. J. Med. Chem. 50 (2007) 3604-3617
    • (2007) J. Med. Chem. , vol.50 , pp. 3604-3617
    • Ye, G.1    Nam, N.H.2    Kumar, A.3    Saleh, A.4    Shenoy, D.B.5    Amiji, M.M.6    Lin, X.7    Sun, G.8    Parang, K.9
  • 3
    • 0035937124 scopus 로고    scopus 로고
    • Arginine-rich peptides. An abundant source of membrane-permeable peptides having potential as carriers for intracellular protein delivery
    • Futaki S., Suzuki T., Ohashi W., Yagami T., Tanaka S., Ueda K., and Sugiura Y. Arginine-rich peptides. An abundant source of membrane-permeable peptides having potential as carriers for intracellular protein delivery. J. Biol. Chem. 276 (2001) 5836-5840
    • (2001) J. Biol. Chem. , vol.276 , pp. 5836-5840
    • Futaki, S.1    Suzuki, T.2    Ohashi, W.3    Yagami, T.4    Tanaka, S.5    Ueda, K.6    Sugiura, Y.7
  • 5
    • 34848892144 scopus 로고    scopus 로고
    • Cell penetrating peptides: intracellular pathways and pharmaceutical perspectives
    • Patel L.N., Zaro J.L., and Shen W.C. Cell penetrating peptides: intracellular pathways and pharmaceutical perspectives. Pharmaceut. Res. 24 (2007) 1977-1992
    • (2007) Pharmaceut. Res. , vol.24 , pp. 1977-1992
    • Patel, L.N.1    Zaro, J.L.2    Shen, W.C.3
  • 6
    • 45749120326 scopus 로고    scopus 로고
    • Cell-penetrating peptides as delivery vehicles for biology and medicine
    • Stewart K.M., Horton K.L., and Kelley S.O. Cell-penetrating peptides as delivery vehicles for biology and medicine. Org. Biomol. Chem. 6 (2008) 2242-2255
    • (2008) Org. Biomol. Chem. , vol.6 , pp. 2242-2255
    • Stewart, K.M.1    Horton, K.L.2    Kelley, S.O.3
  • 7
    • 3843092828 scopus 로고    scopus 로고
    • Chances and pitfalls of cell penetrating peptides for cellular drug delivery
    • Trehin R., and Merkle H.P. Chances and pitfalls of cell penetrating peptides for cellular drug delivery. Eur. J. Pharm. Biopharm. 58 (2004) 209-223
    • (2004) Eur. J. Pharm. Biopharm. , vol.58 , pp. 209-223
    • Trehin, R.1    Merkle, H.P.2
  • 8
    • 56049093057 scopus 로고    scopus 로고
    • Cell-penetrating and cell-targeting peptides in drug delivery
    • Vives E., Schmidt J., and Pelegrin A. Cell-penetrating and cell-targeting peptides in drug delivery. BBA-Rev. Cancer 1786 (2008) 126-138
    • (2008) BBA-Rev. Cancer , vol.1786 , pp. 126-138
    • Vives, E.1    Schmidt, J.2    Pelegrin, A.3
  • 9
    • 23944483437 scopus 로고    scopus 로고
    • Cell-penetrating peptides: tools for intracellular delivery of therapeutics
    • Deshayes S., Morris M.C., Divita G., and Heitz F. Cell-penetrating peptides: tools for intracellular delivery of therapeutics. Cell Mol. Life Sci. 62 (2005) 1839-1849
    • (2005) Cell Mol. Life Sci. , vol.62 , pp. 1839-1849
    • Deshayes, S.1    Morris, M.C.2    Divita, G.3    Heitz, F.4
  • 10
    • 27744557054 scopus 로고    scopus 로고
    • Cell-penetrating peptides: mechanisms and applications
    • El-Andaloussi S., Holm T., and Langel U. Cell-penetrating peptides: mechanisms and applications. Curr. Pharm. Des. 11 (2005) 3597-3611
    • (2005) Curr. Pharm. Des. , vol.11 , pp. 3597-3611
    • El-Andaloussi, S.1    Holm, T.2    Langel, U.3
  • 11
    • 33947393032 scopus 로고    scopus 로고
    • Antimicrobial peptides: an overview of a promising class of therapeutics
    • Giuliani A., Pirri G., and Nicoletto S.F. Antimicrobial peptides: an overview of a promising class of therapeutics. Cent. Eur. J. Biol. 2 (2007) 1-33
    • (2007) Cent. Eur. J. Biol. , vol.2 , pp. 1-33
    • Giuliani, A.1    Pirri, G.2    Nicoletto, S.F.3
  • 12
    • 52649085937 scopus 로고    scopus 로고
    • Synthetic mimics of antimicrobial peptides
    • Som A., Vemparala S., Ivanov I., and Tew G.N. Synthetic mimics of antimicrobial peptides. Biopolymers 90 (2008) 83-93
    • (2008) Biopolymers , vol.90 , pp. 83-93
    • Som, A.1    Vemparala, S.2    Ivanov, I.3    Tew, G.N.4
  • 13
    • 45149099005 scopus 로고    scopus 로고
    • Antibacterial nanomedicine
    • Yacoby I., and Benhar I. Antibacterial nanomedicine. Nanomedicine 3 (2008) 329-341
    • (2008) Nanomedicine , vol.3 , pp. 329-341
    • Yacoby, I.1    Benhar, I.2
  • 14
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 415 (2002) 389-395
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 15
    • 33748947334 scopus 로고    scopus 로고
    • Detergent-like actions of linear amphipathic cationic antimicrobial peptides
    • Bechinger B., and Lohner K. Detergent-like actions of linear amphipathic cationic antimicrobial peptides. Biochim. Biophys. Acta 1758 (2006) 1529-1539
    • (2006) Biochim. Biophys. Acta , vol.1758 , pp. 1529-1539
    • Bechinger, B.1    Lohner, K.2
  • 16
    • 70350040736 scopus 로고    scopus 로고
    • Cell penetrating peptides: how do they do it?
    • Herce H.D., and Garcia A.E. Cell penetrating peptides: how do they do it?. J. Biol. Phys. 33 (2007) 345-356
    • (2007) J. Biol. Phys. , vol.33 , pp. 345-356
    • Herce, H.D.1    Garcia, A.E.2
  • 17
    • 38949116621 scopus 로고    scopus 로고
    • Thermodynamic studies and binding mechanisms of cell-penetrating peptides with lipids and glycosaminoglycans
    • Ziegler A. Thermodynamic studies and binding mechanisms of cell-penetrating peptides with lipids and glycosaminoglycans. Adv. Drug Del. Rev. 60 (2008) 580-597
    • (2008) Adv. Drug Del. Rev. , vol.60 , pp. 580-597
    • Ziegler, A.1
  • 18
    • 38049092119 scopus 로고    scopus 로고
    • Reviewing biophysical and cell biological methodologies in cell-penetrating peptide (CPP) research
    • Herbig M.E., Welter K.M., and Merkle H.A. Reviewing biophysical and cell biological methodologies in cell-penetrating peptide (CPP) research. Crit. Rev. Ther. Drug Carrier Syst. 24 (2007) 203-255
    • (2007) Crit. Rev. Ther. Drug Carrier Syst. , vol.24 , pp. 203-255
    • Herbig, M.E.1    Welter, K.M.2    Merkle, H.A.3
  • 19
    • 27744528180 scopus 로고    scopus 로고
    • Endocytosis and cationic cell-penetrating peptides-a merger of concepts and methods
    • Fotin-Mleczek M., Fischer R., and Brock R. Endocytosis and cationic cell-penetrating peptides-a merger of concepts and methods. Curr. Pharm. Des. 11 (2005) 3613-3628
    • (2005) Curr. Pharm. Des. , vol.11 , pp. 3613-3628
    • Fotin-Mleczek, M.1    Fischer, R.2    Brock, R.3
  • 20
    • 0036159271 scopus 로고    scopus 로고
    • Different mechanisms for cellular internalization of the HIV-1 Tat-derived cell penetrating peptide and recombinant proteins fused to Tat
    • Silhol M., Tyagi M., Giacca M., Lebleu B., and Vives E. Different mechanisms for cellular internalization of the HIV-1 Tat-derived cell penetrating peptide and recombinant proteins fused to Tat. Eur. J. Biochem. 269 (2002) 494-501
    • (2002) Eur. J. Biochem. , vol.269 , pp. 494-501
    • Silhol, M.1    Tyagi, M.2    Giacca, M.3    Lebleu, B.4    Vives, E.5
  • 21
    • 0029982569 scopus 로고    scopus 로고
    • Cell internalization of the third helix of the Antennapedia homeodomain is receptor-independent
    • Derossi D., Calvet S., Trembleau A., Brunissen A., Chassaing G., and 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
  • 25
    • 33846434072 scopus 로고    scopus 로고
    • Stability of cell-penetrating peptide-morpholino oligomer conjugates in human serum and in cells
    • Youngblood D.S., Hatlevig S.A., Hassinger J.N., Iversen P.L., and Moulton H.M. Stability of cell-penetrating peptide-morpholino oligomer conjugates in human serum and in cells. Bioconjug. Chem. 18 (2007) 50-60
    • (2007) Bioconjug. Chem. , vol.18 , pp. 50-60
    • Youngblood, D.S.1    Hatlevig, S.A.2    Hassinger, J.N.3    Iversen, P.L.4    Moulton, H.M.5
  • 26
    • 42149194279 scopus 로고    scopus 로고
    • Arginine-rich cell penetrating peptides: design, structure-activity, and applications to alter pre-mRNA splicing by steric-block oligonucleotides
    • Abes R., Arzumanov A., Moulton H., Abes S., Ivanova G., Gait M.J., Iversen P., and Lebleu B. Arginine-rich cell penetrating peptides: design, structure-activity, and applications to alter pre-mRNA splicing by steric-block oligonucleotides. J. Pept. Sci. 14 (2008) 455-460
    • (2008) J. Pept. Sci. , vol.14 , pp. 455-460
    • Abes, R.1    Arzumanov, A.2    Moulton, H.3    Abes, S.4    Ivanova, G.5    Gait, M.J.6    Iversen, P.7    Lebleu, B.8
  • 28
    • 26044439375 scopus 로고    scopus 로고
    • Phase behavior and nanoscale structure of phospholipid membranes incorporated with acylated C-14-peptides
    • Pedersen T.B., Kaasgaard T., Jensen M.O., Frokjaer S., Mouritsen O.G., and Jorgensen K. Phase behavior and nanoscale structure of phospholipid membranes incorporated with acylated C-14-peptides. Biophys. J. 89 (2005) 2494-2503
    • (2005) Biophys. J. , vol.89 , pp. 2494-2503
    • Pedersen, T.B.1    Kaasgaard, T.2    Jensen, M.O.3    Frokjaer, S.4    Mouritsen, O.G.5    Jorgensen, K.6
  • 29
    • 0034778935 scopus 로고    scopus 로고
    • Association of acylated cationic decapeptides with dipalmitoylphosphatidylserine-dipalmitoyl-phosphatidylcholine lipid membranes
    • Pedersen T.B., Sabra M.C., Frokjaer S., Mouritsen O.G., and Jorgensen K. Association of acylated cationic decapeptides with dipalmitoylphosphatidylserine-dipalmitoyl-phosphatidylcholine lipid membranes. Chem. Phys. Lipids 113 (2001) 83-95
    • (2001) Chem. Phys. Lipids , vol.113 , pp. 83-95
    • Pedersen, T.B.1    Sabra, M.C.2    Frokjaer, S.3    Mouritsen, O.G.4    Jorgensen, K.5
  • 30
    • 0032578027 scopus 로고    scopus 로고
    • Phases and phase transitions of the phosphatidylcholines
    • Koynova R., and Caffrey M. Phases and phase transitions of the phosphatidylcholines. Biochim. Biophys. Acta 1376 (1998) 91-145
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 91-145
    • Koynova, R.1    Caffrey, M.2
  • 31
    • 0030724793 scopus 로고    scopus 로고
    • The mixing behavior of pseudobinary phosphatidylcholine phosphatidylglycerol mixtures as a function of pH and chain length
    • Garidel P., Johann C., Mennicke L., and Blume A. The mixing behavior of pseudobinary phosphatidylcholine phosphatidylglycerol mixtures as a function of pH and chain length. Eur. Biophys. J. Biophys. Lett. 26 (1997) 447-459
    • (1997) Eur. Biophys. J. Biophys. Lett. , vol.26 , pp. 447-459
    • Garidel, P.1    Johann, C.2    Mennicke, L.3    Blume, A.4
  • 32
    • 77956685290 scopus 로고    scopus 로고
    • Coupling of chain melting and bilayer structure: domains, rafts, elasticity and fusion
    • Tien H.T., and Ottova-Leitmannova A. (Eds), Elsevier, Amsterdam
    • Heimburg T. Coupling of chain melting and bilayer structure: domains, rafts, elasticity and fusion. In: Tien H.T., and Ottova-Leitmannova A. (Eds). Planar Lipid Bilayers (BLMs) and their Applications (2003), Elsevier, Amsterdam 269-293
    • (2003) Planar Lipid Bilayers (BLMs) and their Applications , pp. 269-293
    • Heimburg, T.1
  • 33
    • 0035306147 scopus 로고    scopus 로고
    • Histogram method to obtain heat capacities in lipid monolayers, curved bilayers, and membranes containing peptides
    • Ivanova V.P., and Heimburg T. Histogram method to obtain heat capacities in lipid monolayers, curved bilayers, and membranes containing peptides. Phys. Rev. E 6304 (2001)
    • (2001) Phys. Rev. E , vol.6304
    • Ivanova, V.P.1    Heimburg, T.2
  • 34
    • 38049156027 scopus 로고    scopus 로고
    • Molecular dynamics simulations suggest a mechanism for translocation of the HIV-1 TAT peptide across lipid membranes
    • Herce H.D., and Garcia A.E. Molecular dynamics simulations suggest a mechanism for translocation of the HIV-1 TAT peptide across lipid membranes. Proc. Natl. Acad. Sci. U.S.A. 104 (2007) 20805-20810
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 20805-20810
    • Herce, H.D.1    Garcia, A.E.2
  • 35
    • 0016712926 scopus 로고
    • Effects of proteins on thermotropic phase transitions of phospholipid membranes
    • Papahadjopoulos D., Moscarello M., Eylar E.H., and Isac T. Effects of proteins on thermotropic phase transitions of phospholipid membranes. Biochim. Biophys. Acta 401 (1975) 317-335
    • (1975) Biochim. Biophys. Acta , vol.401 , pp. 317-335
    • Papahadjopoulos, D.1    Moscarello, M.2    Eylar, E.H.3    Isac, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.