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Volumn 14, Issue 23, 2014, Pages 2647-2661

Membrane-targeted self-assembling cyclic peptide nanotubes

Author keywords

Antimicrobials; Ion channels; Membrane; Nanotubes; Peptide; Self assembling

Indexed keywords

ANTIINFECTIVE AGENT; CYCLOPEPTIDE; PEPTIDE NANOTUBE; SELF ASSEMBLED CYCLIC PEPTIDE NANOTUBE; UNCLASSIFIED DRUG; CARBOXYLIC ACID; CYCLOALKANE DERIVATIVE; ION CHANNEL; NANOTUBE; PORE FORMING CYTOTOXIC PROTEIN;

EID: 84926340613     PISSN: 15680266     EISSN: 18734294     Source Type: Journal    
DOI: 10.2174/1568026614666141215143431     Document Type: Article
Times cited : (29)

References (140)
  • 2
    • 84926301540 scopus 로고    scopus 로고
    • Some enzymes just need a space of their own
    • Kang, S.; Douglas, T. Some enzymes just need a space of their own. Science, 2009, 327, 42-43
    • (2009) Science , vol.327 , pp. 42-43
    • Kang, S.1    Douglas, T.2
  • 3
    • 51049122765 scopus 로고    scopus 로고
    • Lab-on-achip in vitro Compartmentalization Technologies for Protein Studies
    • Werther, M.; Seitz, H. Eds. Berlin, Heidelberg: Springer Berlin Heidelberg
    • Zhu, Y.; Power, B. E. Lab-on-achip in vitro Compartmentalization Technologies for Protein Studies. In Protein-Protein interactions Advances in Biochemical Engineering/Biotechnology; Werther, M.; Seitz, H. Eds. Berlin, Heidelberg: Springer Berlin Heidelberg; 2008, Vol. 11, pp. 81
    • (2008) Protein-Protein Interactions Advances in Biochemical Engineering/Biotechnology , vol.11 , pp. 81
    • Zhu, Y.1    Power, B.E.2
  • 4
    • 33745423084 scopus 로고    scopus 로고
    • Overview: Methods and applications for droplet compartmentalization of biology
    • Leamon, J.H.; Link, D.R.; Egholm, M.; Rothberg, J.M. Overview: methods and applications for droplet compartmentalization of biology. Nature Methods, 2006, 3, 541–543.
    • (2006) Nature Methods , vol.3 , pp. 541-543
    • Leamon, J.H.1    Link, D.R.2    Egholm, M.3    Rothberg, J.M.4
  • 5
    • 84926330106 scopus 로고    scopus 로고
    • eds. Biotechnological Applications of Lipid Microstructures, Plenum, 1988, New York
    • [2] Gaber, B.P.; Schnur J.M.; Chapman, D. eds. Biotechnological Applications of Lipid Microstructures, Plenum, 1988, New York
    • Gaber, B.P.1    Schnur, J.M.2    Chapman, D.3
  • 6
    • 0008790944 scopus 로고
    • From Physics to Applications Elsevier, Amsterdam
    • Lasic, D.D. Liposomes: From Physics to Applications Elsevier, 1993, Amsterdam
    • (1993) Liposomes
    • Lasic, D.D.1
  • 7
    • 0002056886 scopus 로고
    • Preparation and use of liposomes as models of biological membranes
    • Bangham, A.D.; Hill, M.W.; Miller, N.G.A. Preparation and use of liposomes as models of biological membranes. Methods Membr. Biol., 1973, 1, 1–68.
    • (1973) Methods Membr. Biol. , vol.1 , pp. 1-68
    • Bangham, A.D.1    Hill, M.W.2    Miller, N.3
  • 8
    • 28544453561 scopus 로고    scopus 로고
    • Principles of selective ion transport in channels and pumps
    • [3] Gouaux, E.; MacKinnon, R. Principles of selective ion transport in channels and pumps. Science 2005, 310, 1461-1465
    • (2005) Science , vol.310 , pp. 1461-1465
    • Gouaux, E.1    Mackinnon, R.2
  • 9
    • 0035801339 scopus 로고    scopus 로고
    • Ligand-gated ion channels
    • Hucho, F.; Weise, C. Ligand-gated ion channels. Angew. Chem. Int. Ed., 2001, 40, 3100-3116.
    • (2001) Angew. Chem. Int. Ed , vol.40 , pp. 3100-3116
    • Hucho, F.1    Weise, C.2
  • 10
    • 84926356706 scopus 로고    scopus 로고
    • For some of the latest studies see special number in Acc
    • [4] For some of the latest studies see special number in Acc. Chem. Res., 2013, 46, 2741–3008
    • (2013) Chem. Res. , vol.46 , pp. 2741-3008
  • 11
    • 80053991652 scopus 로고    scopus 로고
    • Ionic conductance of synthetic channels: Analysis, lessons, and recommendations
    • Chui, J.K.W.; Fyles, T.M. Ionic conductance of synthetic channels: analysis, lessons, and recommendations. Chem. Soc. Rev., 2011, 41, 148–175
    • (2011) Chem. Soc. Rev. , vol.41 , pp. 148-175
    • Chui, J.1    Fyles, T.M.2
  • 12
    • 33846666853 scopus 로고    scopus 로고
    • Synthetic ion channels in bilayer membranes
    • Fyles, T.M. Synthetic ion channels in bilayer membranes. Chem. Soc. Rev., 2007, 36, 335–347
    • (2007) Chem. Soc. Rev. , vol.36 , pp. 335-347
    • Fyles, T.M.1
  • 14
    • 0032007854 scopus 로고    scopus 로고
    • Cationic peptides: A new source of antibiotics
    • [5] Hancock, R.E.; Lehrer, R. Cationic peptides: a new source of antibiotics. Trends Biotechnol., 1998, 16, 82-88
    • (1998) Trends Biotechnol. , vol.16 , pp. 82-88
    • Hancock, R.E.1    Lehrer, R.2
  • 15
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff, M. Antimicrobial peptides of multicellular organisms. Nature, 2002, 415, 389-395
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 18
    • 0036948138 scopus 로고    scopus 로고
    • Mode of action of membrane active antimicrobial peptides
    • Shai, Y. Mode of action of membrane active antimicrobial peptides. Biopol. (Peptide Sci.) 2002, 66, 236-248.
    • (2002) Biopol. (Peptide Sci.) , vol.66 , pp. 236-248
    • Shai, Y.1
  • 20
    • 79956294243 scopus 로고    scopus 로고
    • Crystal structure of the Vibrio cholerae cytolysin heptamer reveals common features among disparate pore-forming toxins
    • Olson, S.; De, R. Crystal structure of the Vibrio cholerae cytolysin heptamer reveals common features among disparate pore-forming toxins. Proc. Natl. Acad. Sci. USA, 2011, 108, 7385-7390
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 7385-7390
    • Olson, S.1    De, R.2
  • 21
    • 66649132042 scopus 로고    scopus 로고
    • The structure of a cytolytic -helical toxin pore reveals its assembly mechanism
    • Mueller, M.; Grauschopf, U.; Maier, T.; Glockshuber, R.; Ban, N. The structure of a cytolytic -helical toxin pore reveals its assembly mechanism. Nature, 2009, 459, 726-730
    • (2009) Nature , vol.459 , pp. 726-730
    • Mueller, M.1    Grauschopf, U.2    Maier, T.3    Glockshuber, R.4    Ban, N.5
  • 22
    • 4644355909 scopus 로고    scopus 로고
    • Crystal Structure of Leucotoxin S Component: New insight into the staphylococcal.barrel pore-forming toxins
    • Guillet, V.; Roblin, P.; Werner, S.; Coraiola, M.; Menestrina, G.; Monteil, H.; Prévost, G.; Mourey, L. Crystal Structure of Leucotoxin S Component: New insight into the staphylococcal.barrel pore-forming toxins. J. Biol. Chem., 2004, 279, 41028-41037
    • (2004) J. Biol. Chem. , vol.279 , pp. 41028-41037
    • Guillet, V.1    Roblin, P.2    Werner, S.3    Coraiola, M.4    Menestrina, G.5    Monteil, H.6    Prévost, G.7    Mourey, L.8
  • 23
    • 0030447720 scopus 로고    scopus 로고
    • Structure of Staphylococcal _-Hemolysin, a heptameric transmembrane pore
    • Song, L.; Hobaugh, M.R.; Shustak, C.; Cheley, S.; Bayley, H.; Gouaux, J.E. Structure of Staphylococcal _-Hemolysin, a heptameric transmembrane pore. Science, 1996, 274, 1859-1865
    • (1996) Science , vol.274 , pp. 1859-1865
    • Song, L.1    Hobaugh, M.R.2    Shustak, C.3    Cheley, S.4    Bayley, H.5    Gouaux, J.E.6
  • 24
    • 0027976196 scopus 로고
    • Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states
    • Parker, M.W.; Buckley, J.T.; Postma, J.P.M.; Tucker, A.D.; Leonard, K.; Pattus, F.; Tsernoglou, D. Structure of the Aeromonas toxin proaerolysin in its water-soluble and membrane-channel states. Nature, 1994, 367, 292-295
    • (1994) Nature , vol.367 , pp. 292-295
    • Parker, M.W.1    Buckley, J.T.2    Postma, J.3    Tucker, A.D.4    Leonard, K.5    Pattus, F.6    Tsernoglou, D.7
  • 25
    • 0031457628 scopus 로고    scopus 로고
    • Toxin structure: Part of a hole
    • Bayley H. Toxin structure: Part of a hole? Curr. Biol., 1997, 7, R763-R767.
    • (1997) Curr. Biol. , vol.7 , pp. 763-767
    • Bayley, H.1
  • 26
    • 33845699790 scopus 로고    scopus 로고
    • Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies
    • [8] Hancock, R.E.W.; Sahl, H.-G. Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies. Nat. Biotechnol., 2006, 24, 1551-1557
    • (2006) Nat. Biotechnol. , vol.24 , pp. 1551-1557
    • Hancock, R.1    Sahl, H.-G.2
  • 27
    • 60749118913 scopus 로고    scopus 로고
    • Antimicrobial peptides: Linking partition, activity and high membrane-bound concentrations
    • Melo, M.N.; Ferre, R.; Castanho, M.A.R.B. Antimicrobial peptides: Linking partition, activity and high membrane-bound concentrations. Nat. Rev. Microbiol., 2009, 7, 245-250.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 245-250
    • Melo, M.N.1    Ferre, R.2    Castanho, M.3
  • 28
    • 84857411069 scopus 로고    scopus 로고
    • Designing antimicrobial peptides: Form follows function. Nat
    • [9] Fjell, C.D.; Hiss, J.A.; Hancock, R.E.W.; Schneider, G. Designing antimicrobial peptides: form follows function. Nat. Rev. Drug Discov., 2012, 11, 37-51
    • (2012) Rev. Drug Discov. , vol.11 , pp. 37-51
    • Fjell, C.D.1    Hiss, J.A.2    Hancock, R.3    Schneider, G.4
  • 29
    • 1042278915 scopus 로고    scopus 로고
    • The relationship between peptide structure and antibacterial activity
    • Powers, J.P.; Hancock, R.E. The relationship between peptide structure and antibacterial activity. Peptides, 2003, 24, 1681-1691.
    • (2003) Peptides , vol.24 , pp. 1681-1691
    • Powers, J.P.1    Hancock, R.E.2
  • 30
    • 0032693639 scopus 로고    scopus 로고
    • Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes
    • [10] Matsuzaki, K. Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes. Biochim. Biophys. Acta., 1999, 1462, 1–10
    • (1999) Biochim. Biophys. Acta. , vol.1462 , pp. 1-10
    • Matsuzaki, K.1
  • 31
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria? Nat
    • Brogden, K.A. Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat. Rev. Microbiol., 2005, 3, 238-250.
    • (2005) Rev. Microbiol. , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 32
    • 84885183690 scopus 로고    scopus 로고
    • Combating multidrug-resistant bacteria: Current strategies for the discovery of novel antibacterials
    • [11] O'Connell, K.M.G.; Hodgkinson, J.T.; Sore, H.F.; Welch, M.; Salmond, G.P.C.; Spring, D.R. Combating multidrug-resistant bacteria: Current strategies for the discovery of novel antibacterials. Angew. Chem. Int. Ed., 2013, 52, 10706-10733
    • (2013) Angew. Chem. Int. Ed , vol.52 , pp. 10706-10733
    • O'connell, K.1    Hodgkinson, J.T.2    Sore, H.F.3    Welch, M.4    Salmond, G.5    Spring, D.R.6
  • 33
    • 84887769885 scopus 로고    scopus 로고
    • Time to deal with antibiotics
    • Kennedy, D. Time to deal with antibiotics. Science, 2013, 342, 777-777
    • (2013) Science , vol.342 , pp. 777
    • Kennedy, D.1
  • 34
    • 84862001187 scopus 로고    scopus 로고
    • Emerging trends in macromolecular antimicrobials to fight multi-drug-resistant infections. Nano
    • Engler, A.C.; Wiradharma, N.; Ong, Z.Y.; Coady, D.J.; Hedrick, J.L.; Yang, Y.-Y. Emerging trends in macromolecular antimicrobials to fight multi-drug-resistant infections. Nano. Today, 2012, 7, 201-222
    • (2012) Today , vol.7 , pp. 201-222
    • Engler, A.C.1    Wiradharma, N.2    Ong, Z.Y.3    Coady, D.J.4    Hedrick, J.L.5    Yang, Y.-Y.6
  • 35
    • 79953740494 scopus 로고    scopus 로고
    • Fix the antibiotics pipeline
    • Cooper, M.A.; Shlaes, D. Fix the antibiotics pipeline. Nature, 2011, 472, 32-32
    • (2011) Nature , vol.472 , pp. 32
    • Cooper, M.A.1    Shlaes, D.2
  • 36
    • 84861423745 scopus 로고    scopus 로고
    • Recover the lost art of drug discovery
    • Lewis, K. Recover the lost art of drug discovery. Nature, 2012, 485, 439-440
    • (2012) Nature , vol.485 , pp. 439-440
    • Lewis, K.1
  • 38
    • 65249146929 scopus 로고    scopus 로고
    • Multidrug resistance in bacteria
    • Nikaido, H. Multidrug resistance in bacteria. Annu. Rev. Biochem., 2009, 78, 119-146
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 119-146
    • Nikaido, H.1
  • 39
    • 69249083586 scopus 로고    scopus 로고
    • Waves of resistance: Staphylococcus aureus in the antibiotic era
    • Chambers, H.F.; Deleo, F.R. Waves of resistance: Staphylococcus aureus in the antibiotic era. Nat. Rev. Microbiol., 2009, 7, 629-641
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 629-641
    • Chambers, H.F.1    Deleo, F.R.2
  • 40
    • 33845903833 scopus 로고    scopus 로고
    • Drugs for bad bugs: Confronting the challenges of antibacterial discovery. Nat
    • Payne, D.J.; Gwynn, M.N.; Holmes, D.J.; Pompliano, D.L. Drugs for bad bugs: confronting the challenges of antibacterial discovery. Nat. Rev. Drug Discov., 2007, 6, 29-40
    • (2007) Rev. Drug Discov. , vol.6 , pp. 29-40
    • Payne, D.J.1    Gwynn, M.N.2    Holmes, D.J.3    Pompliano, D.L.4
  • 41
    • 0038665502 scopus 로고    scopus 로고
    • Antimicrobial resistance: The example of Staphylococcus aureus
    • Lowy, F.D. Antimicrobial resistance: the example of Staphylococcus aureus. J. Clin. Invest., 2003, 111, 1265-1273.
    • (2003) J. Clin. Invest. , vol.111 , pp. 1265-1273
    • Lowy, F.D.1
  • 43
    • 78651445030 scopus 로고    scopus 로고
    • Synthetic cationic amphiphilic _-helical peptides as antimicrobial agents
    • Wiradharma, N.; Khoe, U.; Hauser, C.A.; Seow, S.V.; Zhang, S.; Yang, Y.Y. Synthetic cationic amphiphilic _-helical peptides as antimicrobial agents. Biomaterials, 2011, 32, 2204-2212
    • (2011) Biomaterials , vol.32 , pp. 2204-2212
    • Wiradharma, N.1    Khoe, U.2    Hauser, C.A.3    Seow, S.V.4    Zhang, S.5    Yang, Y.Y.6
  • 45
    • 84856460625 scopus 로고    scopus 로고
    • Therapeutic potential of host defense peptides in antibiotic-resistant infections
    • Afacan, N.J.; Yeung, A.T.; Pena, O.M.; Hancock, R.E. Therapeutic potential of host defense peptides in antibiotic-resistant infections. Curr. Pharm. Des., 2012, 18, 807-819.
    • (2012) Curr. Pharm. Des. , vol.18 , pp. 807-819
    • Afacan, N.J.1    Yeung, A.T.2    Pena, O.M.3    Hancock, R.E.4
  • 46
    • 23644446162 scopus 로고    scopus 로고
    • The channelopathies: Novel insights into molecular and genetic mechanisms of human disease
    • [13] Kass, R.S. The channelopathies: novel insights into molecular and genetic mechanisms of human disease. J. Clin. Inves. 2005, 115, 1986-1989
    • (2005) J. Clin. Inves , vol.115 , pp. 1986-1989
    • Kass, R.S.1
  • 47
    • 84926297521 scopus 로고    scopus 로고
    • dis., Academic Press
    • Gilman, S. Ed. Neurobiol. dis., Academic Press. 2010, pp. 319.
    • (2010) Neurobiol , pp. 319
    • Gilman, S.1
  • 48
    • 84926360680 scopus 로고    scopus 로고
    • Synthesis of Supramolecular Nanotubes (In Supramolecular Chemistry: From Molecules to Nanomaterials) (Gale, P. A; Steed, J. W. Eds.) John Wiley & Sons Ltd: New York, 2012
    • [14] Garcia-Fandiño, R.; Amorín, M.; Granja, J.R. Synthesis of Supramolecular Nanotubes (In Supramolecular Chemistry: From Molecules to Nanomaterials) (Gale, P. A; Steed, J. W. Eds.) John Wiley & Sons Ltd: New York, 2012, vol. 5, pp. 2149-2182
    • , vol.5 , pp. 2149-2182
    • Garcia-Fandiño, R.1    Amorín, M.2    Granja, J.R.3
  • 49
    • 84870156651 scopus 로고    scopus 로고
    • Design and properties of functional nanotubes from the selfassembly of cyclic peptide templates
    • Chapman, R.; Danial, M.; Koh, M.L.; Jolliffe, K.A.; Perrier, S. Design and properties of functional nanotubes from the selfassembly of cyclic peptide templates. Chem. Soc. Rev., 2012, 41, 6023-6041
    • (2012) Chem. Soc. Rev. , vol.41 , pp. 6023-6041
    • Chapman, R.1    Danial, M.2    Koh, M.L.3    Jolliffe, K.A.4    Perrier, S.5
  • 50
    • 77951613692 scopus 로고    scopus 로고
    • Towards functional bionanomaterials based on self-assembling cyclic peptide nanotubes
    • Brea, R.J.; Reiriz, C.; Granja, J.R. Towards functional bionanomaterials based on self-assembling cyclic peptide nanotubes. Chem. Soc. Rev., 2010, 39, 1448-1456
    • (2010) Chem. Soc. Rev. , vol.39 , pp. 1448-1456
    • Brea, R.J.1    Reiriz, C.2    Granja, J.R.3
  • 52
    • 0027703505 scopus 로고
    • Self-assembling organic nanotubes based on a cyclic peptide architecture
    • [15] Ghadiri, M.R.; Granja, J.R.; Milligan, R.A.; Mcree, D.E.; Khazanovich, N. Self-assembling organic nanotubes based on a cyclic peptide architecture. Nature, 1993, 366, 324-327
    • (1993) Nature , vol.366 , pp. 324-327
    • Ghadiri, M.R.1    Granja, J.R.2    Milligan, R.A.3    McRee, D.E.4    Khazanovich, N.5
  • 54
    • 1642280493 scopus 로고    scopus 로고
    • Self-assembling peptide nanotubes from enantiomeric pairs of cyclic peptides with alternating D and L-amino acid residues
    • Rosenthal, K.; Svensson, G.; Undén, A. Self-assembling peptide nanotubes from enantiomeric pairs of cyclic peptides with alternating D and L-amino acid residues. J. Am. Chem. Soc., 2004, 126, 3372-3373.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 3372-3373
    • Rosenthal, K.1    Svensson, G.2    Undén, A.3
  • 55
  • 56
    • 0029167845 scopus 로고
    • Sheet Peptide Architecture: Measuring the Relative Stability of Parallel vs. Antiparallel -Sheets
    • Kobayashi, K.; Granja, J.R.; Ghadiri, M.R. Sheet Peptide Architecture: Measuring the Relative Stability of Parallel vs. Antiparallel -Sheets. Angew. Chem., Int. Ed. Engl., 1995, 34, 95-98.
    • (1995) Angew. Chem., Int. Ed. Engl., , vol.34 , pp. 95-98
    • Kobayashi, K.1    Granja, J.R.2    Ghadiri, M.R.3
  • 57
    • 0028459606 scopus 로고
    • Nanoscale Tubular Ensembles with Specified Internal Diameters. Design of a Self-Assembled Nanotube with a 13-Å Pore
    • [17] Khazanovich, N.; Granja, J.R.; Mcree, D.E.; Milligan, R.A.; Ghadiri, M.R. Nanoscale Tubular Ensembles with Specified Internal Diameters. Design of a Self-Assembled Nanotube with a 13-Å Pore. J. Am. Chem. Soc., 1994, 116, 6011-6012
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 6011-6012
    • Khazanovich, N.1    Granja, J.R.2    McRee, D.E.3    Milligan, R.A.4    Ghadiri, M.R.5
  • 58
    • 84987340520 scopus 로고
    • On the Stacking of _-Rings: The solution selfassociation behavior of two partially N-methylated cyclo(hexaleucines). Helv. Chim
    • Sun, X.C.; Lorenzi, G. P. On the Stacking of _-Rings: The solution selfassociation behavior of two partially N-methylated cyclo(hexaleucines). Helv. Chim. Acta, 1994, 77, 1520-1526
    • (1994) Acta , vol.77 , pp. 1520-1526
    • Sun, X.C.1    Lorenzi, G.P.2
  • 59
    • 27144476831 scopus 로고    scopus 로고
    • The smallest _,_-peptide nanotubulet segments: Cyclic _,_-tetrapeptide dimers. Org
    • Amorin, M.; Brea, R.J.; Castedo, L.; Granja, J.R. The smallest _,_-peptide nanotubulet segments: Cyclic _,_-tetrapeptide dimers. Org. Lett., 2005, 7, 4681-4684
    • (2005) Lett. , vol.7 , pp. 4681-4684
    • Amorin, M.1    Brea, R.J.2    Castedo, L.3    Granja, J.R.4
  • 60
    • 34547641363 scopus 로고    scopus 로고
    • Large-diameter self-assembled dimers of _,_-cyclic peptides, with the nanotubular solid-state structure of cyclo-[(L-Leu-D-MeN-_-Acp)4-].4CHCl2COOH
    • Brea, R.J.; Castedo, L.; Granja, J.R. Large-diameter self-assembled dimers of _,_-cyclic peptides, with the nanotubular solid-state structure of cyclo-[(L-Leu-D-MeN-_-Acp)4-].4CHCl2COOH. Chem. Commun., 2007, 31, 3267-3269.
    • (2007) Chem. Commun. , vol.31 , pp. 3267-3269
    • Brea, R.J.1    Castedo, L.2    Granja, J.R.3
  • 61
    • 1842410757 scopus 로고    scopus 로고
    • Diffusionlimited size-selective ion sensing based on SAM-supported peptide nanotubes
    • Motesharei, K.; Ghadiri, M.R. Diffusionlimited size-selective ion sensing based on SAM-supported peptide nanotubes. J. Am. Chem. Soc., 1997, 119, 11306-11312
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 11306-11312
    • Motesharei, K.1    Ghadiri, M.R.2
  • 62
    • 0033152135 scopus 로고    scopus 로고
    • Photoswitchable Hydrogen-Bonding in Self-Organized Cylindrical Peptide Systems
    • Vollmer, M.S.; Clark, T.D.; Steinem, C.; Ghadiri, M.R. Photoswitchable Hydrogen-Bonding in Self-Organized Cylindrical Peptide Systems. Angew. Chem. Int. Ed., 1999, 38, 1598-1601
    • (1999) Angew. Chem. Int. Ed , vol.38 , pp. 1598-1601
    • Vollmer, M.S.1    Clark, T.D.2    Steinem, C.3    Ghadiri, M.R.4
  • 63
    • 0034614053 scopus 로고    scopus 로고
    • Cyclic peptides as molecular adapters for a pore-forming protein
    • Sanchez-Quesada, J.; Ghadiri, M.R.; Bayley, H.; Braha, O. Cyclic peptides as molecular adapters for a pore-forming protein. J. Am. Chem. Soc., 2000, 122, 11757-1766
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 11757-11766
    • Sanchez-Quesada, J.1    Ghadiri, M.R.2    Bayley, H.3    Braha, O.4
  • 67
    • 32044443628 scopus 로고    scopus 로고
    • Design of self-assembling peptide nanotubes with delocalized electronic states
    • Ashkenasy, N.; Horne, W.S.; Ghadiri, M.R. Design of self-assembling peptide nanotubes with delocalized electronic states. Small, 2006, 2, 99-102
    • (2006) Small , vol.2 , pp. 99-102
    • Ashkenasy, N.1    Horne, W.S.2    Ghadiri, M.R.3
  • 68
    • 79952849753 scopus 로고    scopus 로고
    • Assemblies of Functional Peptides and Their Applications in Building Blocks for Biosensors
    • de la Rica, R.; Pejoux, C.; Matsui, H. Assemblies of Functional Peptides and Their Applications in Building Blocks for Biosensors. Adv. Funct. Mater., 2011, 21, 1018-1026
    • (2011) Adv. Funct. Mater. , vol.21 , pp. 1018-1026
    • De La Rica, R.1    Pejoux, C.2    Matsui, H.3
  • 69
    • 79951918055 scopus 로고    scopus 로고
    • Subnanometer porous thin films by the co-assembly of nanotube subunits and block copolymers
    • Xu, T.; Zhao, N.; Ren, F.; Hourani, R.; Tsang Lee, M.; Shu, J.Y.; Mao, S.; Helms, B.A. Subnanometer porous thin films by the co-assembly of nanotube subunits and block copolymers. ACS Nano., 2011, 2, 1376-1384
    • (2011) ACS Nano. , vol.2 , pp. 1376-1384
    • Xu, T.1    Zhao, N.2    Ren, F.3    Hourani, R.4    Tsang Lee, M.5    Shu, J.Y.6    Mao, S.7    Helms, B.A.8
  • 70
    • 84855579267 scopus 로고    scopus 로고
    • Charge transport in vertically aligned, self-assembled peptide nanotube junctions
    • Mizrahi, M.; Zakrassov, A.; Lerner-Yardeni, J.; Ashkenasy, N. Charge transport in vertically aligned, self-assembled peptide nanotube junctions. Nanoscale, 2012, 4, 518-524
    • (2012) Nanoscale , vol.4 , pp. 518-524
    • Mizrahi, M.1    Zakrassov, A.2    Lerner-Yardeni, J.3    Ashkenasy, N.4
  • 71
    • 84873298415 scopus 로고    scopus 로고
    • Water-soluble and pH-responsive polymeric nanotubes from cyclic peptide templates
    • Chapman, R.; Warr, G.G.; Perrier, S.; Jolliffe, K.A. Water-soluble and pH-responsive polymeric nanotubes from cyclic peptide templates. Chem.–Eur. J., 2013, 19, 1955-1961.
    • (2013) Chem.–Eur. J. , vol.19 , pp. 1955-1961
    • Chapman, R.1    Warr, G.G.2    Perrier, S.3    Jolliffe, K.A.4
  • 72
    • 84926382434 scopus 로고    scopus 로고
    • Peptide sequences are written using the conventional one-letter code for amino acids, but residues having D stereochemistry are underlined
    • Peptide sequences are written using the conventional one-letter code for amino acids, but residues having D stereochemistry are underlined.
  • 73
    • 0031040358 scopus 로고    scopus 로고
    • Cyclo-_-peptides: Structure and tubular stacking of cyclic tetramers of 3-aminobutanoic acid as determined from powder diffraction data
    • [20] Seebach, D.; Matthews, J.L.; Meden, A.; Wessels, T.; Baerlocher, C.; McCusker, L.B. Cyclo-_-peptides: Structure and tubular stacking of cyclic tetramers of 3-aminobutanoic acid as determined from powder diffraction data. Helv. Chim. Acta., 1997, 80, 173-182
    • (1997) Helv. Chim. Acta. , vol.80 , pp. 173-182
    • Seebach, D.1    Matthews, J.L.2    Meden, A.3    Wessels, T.4    Baerlocher, C.5    McCusker, L.B.6
  • 74
    • 84864504602 scopus 로고    scopus 로고
    • Peptide nanotube composed of cyclic tetra-_-peptide having polydiacetylen
    •  Ishihara, Y.; Kimura, S. Peptide nanotube composed of cyclic tetra-_-peptide having polydiacetylene. Biopolymers, 2012, 98, 155-160
    • (2011) Biopolymer , vol.9 , pp. 155-216
    • Ishihar, Y.1    Kimur, S.2
  • 75
    • 0035905358 scopus 로고    scopus 로고
    • Self-assembly of cyclic peptides into nanotubes and then into highly anisotropic crystalline materials
    • Gauthier, D.; Baillargeon, P.; Drouin, M.; Dory, Y.L. Self-assembly of cyclic peptides into nanotubes and then into highly anisotropic crystalline materials. Angew. Chem. Int. Ed., 2001, 40, 4635-4638
    • Angew. Chem. Int. Ed., 2001 , vol.40 , pp. 4635-4638
    • Gauthier, D.1    Baillargeon, P.2    Drouin, M.3    Dory, Y.L.4
  • 78
    • 0037013980 scopus 로고    scopus 로고
    • Self-assembling organic nanotubes from enantiopure cyclo-N,N'-linked oligoureas: Design, synthesis, and crystal structure
    • Semetey, V.; Didierjean, C.; Briand, J.P.; Aubry, A.; Guichard, G. Self-assembling organic nanotubes from enantiopure cyclo-N,N'-linked oligoureas: Design, synthesis, and crystal structure. Angew. Chem. Int. Ed., 2002, 41, 1895-1898
    • (2002) Angew. Chem. Int. Ed , vol.41 , pp. 1895-1898
    • Semetey, V.1    Didierjean, C.2    Briand, J.P.3    Aubry, A.4    Guichard, G.5
  • 79
    • 60749128718 scopus 로고    scopus 로고
    • Control of duplex formation and columnar self-assembly with heterogeneous amide/urea macrocycles
    • Fischer, L.; Decossas, M.; Briand, J.P.; Didierjean, C.; Guichard, G. Control of duplex formation and columnar self-assembly with heterogeneous amide/urea macrocycles. Angew. Chem. Int. Ed., 2008, 48, 1625-1628
    • (2008) Angew. Chem. Int. Ed , vol.48 , pp. 1625-1628
    • Fischer, L.1    Decossas, M.2    Briand, J.P.3    Didierjean, C.4    Guichard, G.5
  • 81
    • 0037433498 scopus 로고    scopus 로고
    • New cyclic peptide assemblies with hydrophobic cavities: The structural and thermodynamic basis of a new class of peptide nanotubes
    • [21] Amorin, M.; Castedo, L.; Granja, J.R. New cyclic peptide assemblies with hydrophobic cavities: the structural and thermodynamic basis of a new class of peptide nanotubes. J. Am. Chem. Soc., 2003, 125, 2844-2845
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 2844-2845
    • Amorin, M.1    Castedo, L.2    Granja, J.R.3
  • 82
    • 27744590590 scopus 로고    scopus 로고
    • Self-assembled peptide tubelets with 7 Å pores
    • Amorin, M.; Castedo, L.; Granja J.R. Self-assembled peptide tubelets with 7 Å pores. Chem.–Eur. J., 2005, 11, 6543-6551
    • (2005) Chem.–Eur. J. , vol.11 , pp. 6543-6551
    • Amorin, M.1    Castedo, L.2    Granja, J.R.3
  • 85
    • 24944550968 scopus 로고    scopus 로고
    • Methylblocked dimeric _,_-peptide nanotube segments: Formation of a peptide heterodimer through backbone-backbone interactions
    • [22] Brea, R.J.; Amorin, M.; Castedo, L.; Granja, J.R. Methylblocked dimeric _,_-peptide nanotube segments: Formation of a peptide heterodimer through backbone-backbone interactions. Angew. Chem. Int. Ed., 2005, 44, 5710-5713
    • (2005) Angew. Chem. Int. Ed , vol.44 , pp. 5710-5713
    • Brea, R.J.1    Amorin, M.2    Castedo, L.3    Granja, J.R.4
  • 86
    • 78650794230 scopus 로고    scopus 로고
    • Highly efficient and directional homo-and heterodimeric energy transfer materials based on fluorescently derivatized _,_-cyclic octapeptides
    • Brea, R.J.; Pérez-Alvite, M.J.; Panciera, M.; Mosquera, M.; Castedo, L.; Granja, J.R. Highly efficient and directional homo-and heterodimeric energy transfer materials based on fluorescently derivatized _,_-cyclic octapeptides. Chem.–Asian. J., 2011, 6, 110-121.
    • (2011) Chem.–Asian. J. , vol.6 , pp. 110-121
    • Brea, R.J.1    Pérez-Alvite, M.J.2    Panciera, M.3    Mosquera, M.4    Castedo, L.5    Granja, J.R.6
  • 87
    • 33846979505 scopus 로고    scopus 로고
    • Controlling multiple fluorescent signal output in cyclic peptide-based supramolecular systems
    • [23] Brea, R.J.; Vazquez, M.E.; Mosquera, M.; Castedo, L.; Granja, J.R. Controlling multiple fluorescent signal output in cyclic peptide-based supramolecular systems. J. Am. Chem. Soc., 2007, 129, 1653-1657
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 1653-1657
    • Brea, R.J.1    Vazquez, M.E.2    Mosquera, M.3    Castedo, L.4    Granja, J.R.5
  • 90
    • 0028174318 scopus 로고
    • Artificial transmembrane ion channels from self-assembling peptide nanotubes
    • [24] Ghadiri, M.R.; Granja, J.R.; Buehler, L.K. Artificial transmembrane ion channels from self-assembling peptide nanotubes. Nature, 1994, 369, 301-304
    • (1994) Nature , vol.369 , pp. 301-304
    • Ghadiri, M.R.1    Granja, J.R.2    Buehler, L.K.3
  • 91
    • 84890648683 scopus 로고    scopus 로고
    • Ion channel models based on self-assembling cyclic peptide nanotubes
    • Montenegro, J.; Ghadiri, M.R.; Granja, J.R. Ion channel models based on self-assembling cyclic peptide nanotubes. Acc. Chem. Res., 2013, 46, 2955-2965.
    • (2013) Acc. Chem. Res. , vol.46 , pp. 2955-2965
    • Montenegro, J.1    Ghadiri, M.R.2    Granja, J.R.3
  • 92
    • 0029002812 scopus 로고
    • The conformational analysis of peptides using FTIR
    • [25] Haris, P.I.; Chapman, D. The conformational analysis of peptides using FTIR. Biopoly. (Peptide Sci.) 1995, 37, 251-263
    • (1995) Biopoly. (Peptide Sci.) , vol.37 , pp. 251-263
    • Haris, P.I.1    Chapman, D.2
  • 93
    • 0023008334 scopus 로고
    • Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins
    • Krimm, S.; Bandekar, J. Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. Adv. Pro. Chem., 1986, 38, 181-364
    • (1986) Adv. Pro. Chem. , vol.38 , pp. 181-364
    • Krimm, S.1    Bandekar, J.2
  • 94
    • 0026507761 scopus 로고
    • Amide modes and protein conformation
    • Bandekar, J. Amide modes and protein conformation. Biochim. Biophys. Acta, 1992, 1120, 123-143.
    • (1992) Biochim. Biophys. Acta , vol.1120 , pp. 123-143
    • Bandekar, J.1
  • 96
    • 78651026696 scopus 로고
    • The effect of sodium ions on the electrical activity of the giant axon of the squid
    • [27] Hodkin, A.L.; Katz, B. The effect of sodium ions on the electrical activity of the giant axon of the squid. J. Physiol., 1949, 108, 37-77.
    • (1949) J. Physiol. , vol.108 , pp. 37-77
    • Hodkin, A.L.1    Katz, B.2
  • 97
    • 0037189896 scopus 로고    scopus 로고
    • Modulating ion channel properties of transmembrane peptide nanotubes through heteromeric supramolecular assemblies
    • [28] Sanchez-Quesada, J.; Isler, M.; Ghadiri, M.R. Modulating ion channel properties of transmembrane peptide nanotubes through heteromeric supramolecular assemblies. J. Am. Chem. Soc., 2002, 124, 10004-10005.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 10004-10005
    • Sanchez-Quesada, J.1    Isler, M.2    Ghadiri, M.R.3
  • 98
    • 0032481333 scopus 로고    scopus 로고
    • Self-assembling cyclic _3-peptide nanotubes as artificial transmembrane ion channels
    • [29] Clark, T.D.; Buehler, L.K.; Ghadiri, M.R. Self-assembling cyclic _3-peptide nanotubes as artificial transmembrane ion channels. J. Am. Chem. Soc., 1998, 120, 651-656
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 651-656
    • Clark, T.D.1    Buehler, L.K.2    Ghadiri, M.R.3
  • 99
    • 0035197730 scopus 로고    scopus 로고
    • Designer hybrid cyclopeptides for membrane ion transport and tubular structures
    • Ranganathan, D. Designer hybrid cyclopeptides for membrane ion transport and tubular structures. Acc. Chem. Res., 2001, 34, 919-930
    • (2001) Acc. Chem. Res. , vol.34 , pp. 919-930
    • Ranganathan, D.1
  • 100
    • 70450191096 scopus 로고    scopus 로고
    • Anion-macrodipole interactions: Self-assembling oligourea/amide macrocycles as anion Transporters that respond to membrane polarization
    • Hennig, A.; Fischer, L.; Guichard, G.; Matile, S. Anion-macrodipole interactions: Self-assembling oligourea/amide macrocycles as anion Transporters that respond to membrane polarization. J. Am. Chem. Soc., 2009, 131, 16889-16895.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 16889-16895
    • Hennig, A.1    Fischer, L.2    Guichard, G.3    Matile, S.4
  • 101
    • 0027954789 scopus 로고
    • Channel-mediated transport of glucose across lipid bilayers
    • [30] Granja, J.R.; Ghadiri, M.R. Channel-mediated transport of glucose across lipid bilayers. J. Am. Chem. Soc., 1994, 116, 10785-10786
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 10785-10786
    • Granja, J.R.1    Ghadiri, M.R.2
  • 102
    • 0035796637 scopus 로고    scopus 로고
    • A Synthetic pore-mediated transmembrane transport of glutamic acid
    • Sanchez-Quesada, J.; Kim, H.S.; Ghadiri, M.R. A Synthetic pore-mediated transmembrane transport of glutamic acid. Angew. Chem. Int. Ed., 2001, 40, 2503-2506.
    • (2001) Angew. Chem. Int. Ed , vol.40 , pp. 2503-2506
    • Sanchez-Quesada, J.1    Kim, H.S.2    Ghadiri, M.R.3
  • 103
    • 70350639426 scopus 로고    scopus 로고
    • Theoretical characterization of the dynamical behavior and transport properties of _,_-peptide nanotubes in solution
    • [31] García-Fandiño, R.; Granja, J.R.; D'Abramo, M.; Orozco, M. Theoretical characterization of the dynamical behavior and transport properties of _,_-peptide nanotubes in solution. J. Am. Chem. Soc., 2009, 131, 15678-15686
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 15678-15686
    • García-Fandiño, R.1    Granja, J.R.2    D'abramo, M.3    Orozco, M.4
  • 104
    • 84878105183 scopus 로고    scopus 로고
    • Effect of organochloride guest molecules on the stability of homo/hetero self-assembled _,_-cyclic peptide structures: A computational study toward the control of nanotube length
    • García-Fandiño, R.; Granja, J.R. Effect of organochloride guest molecules on the stability of homo/hetero self-assembled _,_-cyclic peptide structures: A computational study toward the control of nanotube length. J. Phys. Chem. C., 2013, 117, 10143-10162.
    • (2013) J. Phys. Chem. C. , vol.117 , pp. 10143-10162
    • García-Fandiño, R.1    Granja, J.R.2
  • 105
    • 84867350967 scopus 로고    scopus 로고
    • Transmembrane ion transport by self-assembling _,_-peptide nanotubes
    • [32] García-Fandiño, R.; Amorín, M.; Castedo, L.; Granja, J.R. Transmembrane ion transport by self-assembling _,_-peptide nanotubes. Chem. Sci., 2012, 3, 3280-3285.
    • (2012) Chem. Sci. , vol.3 , pp. 3280-3285
    • García-Fandiño, R.1    Amorín, M.2    Castedo, L.3    Granja, J.R.4
  • 108
    • 70350097624 scopus 로고    scopus 로고
    • _,_-Cyclic peptide ensembles with a hydroxylated cavity. Org. Biomol
    • Reiriz, C.; Amorín, M.; García-Fandiño, R.; Castedo, L.; Granja, J.R. _,_-Cyclic peptide ensembles with a hydroxylated cavity. Org. Biomol. Chem., 2009, 7, 4358-4361.
    • (2009) Chem. , vol.7 , pp. 4358-4361
    • Reiriz, C.1    Amorín, M.2    García-Fandiño, R.3    Castedo, L.4    Granja, J.R.5
  • 109
    • 84870938851 scopus 로고    scopus 로고
    • Ion channel associated diseases: Overview of molecular mechanisms
    • [35] Zaydman, M.A.; Silva, J.R.; Cui, J. Ion channel associated diseases: Overview of molecular mechanisms. Chem. Rev., 2012, 112, 6319-6333
    • (2012) Chem. Rev. , vol.112 , pp. 6319-6333
    • Zaydman, M.A.1    Silva, J.R.2    Cui, J.3
  • 111
    • 0000750272 scopus 로고
    • Structure and dynamics of self-assembling peptide nanotubes and the channel-mediated water organization and self-diffusion
    • [36] Engels, M.; Bashford, D.; Ghadiri, M.R. Structure and dynamics of self-assembling peptide nanotubes and the channel-mediated water organization and self-diffusion. A molecular dynamics study. J. Am. Chem. Soc., 1995, 117, 9151-9158
    • (1995) A Molecular Dynamics Study. J. Am. Chem. Soc. , vol.117 , pp. 9151-9158
    • Engels, M.1    Bashford, D.2    Ghadiri, M.R.3
  • 112
    • 0141754087 scopus 로고    scopus 로고
    • Molecular dynamics investigation of an oriented cyclic peptide nanotube in
    • Tarek, M.; Maigret, B.; Chipot, C. Molecular dynamics investigation of an oriented cyclic peptide nanotube in DMPC bilayers. Biophys. J., 2003, 85, 2287-2298
    • (2003) DMPC Bilayers. Biophys. J. , vol.85 , pp. 2287-2298
    • Tarek, M.1    Maigret, B.2    Chipot, C.3
  • 113
    • 33846457397 scopus 로고    scopus 로고
    • Steered molecular dynamics studies of the potential of mean force of a Na+ or K+ ion in a cyclic peptide nanotube
    • Hwang, H.; Schatz, G.C.; Ratner, M.A. Steered molecular dynamics studies of the potential of mean force of a Na+ or K+ ion in a cyclic peptide nanotube. J. Phys. Chem. B., 2006, 110, 26448-26460
    • (2006) J. Phys. Chem. B. , vol.110 , pp. 26448-26460
    • Hwang, H.1    Schatz, G.C.2    Ratner, M.A.3
  • 114
    • 33646379364 scopus 로고    scopus 로고
    • Ion current calculations based on three dimensional Poisson_Nernst_Planck theory for a cyclic peptide nanotube
    • Hwang, H.; Schatz, G.C.; Ratner, M.A. Ion current calculations based on three dimensional Poisson_Nernst_Planck theory for a cyclic peptide nanotube. J. Phys. Chem. B., 2006, 110, 6999-7008
    • (2006) J. Phys. Chem. B. , vol.110 , pp. 6999-7008
    • Hwang, H.1    Schatz, G.C.2    Ratner, M.A.3
  • 115
    • 33645526105 scopus 로고    scopus 로고
    • Interaction of a peptide nanotube with a water–membrane interface. Phys
    • Chipot, C.; Tarek, M. Interaction of a peptide nanotube with a water–membrane interface. Phys. Biol., 2006, 3, S20-S25
    • (2006) Biol. , vol.3 , pp. 20-25
    • Chipot, C.1    Tarek, M.2
  • 116
    • 34848923636 scopus 로고    scopus 로고
    • Energetics of Ion Transport in a Peptide Nanotube
    • Dehez, F.; Tarek, M.; Chipot, C. Energetics of Ion Transport in a Peptide Nanotube. J. Phys. Chem. B., 2007, 111, 10633-10635
    • (2007) J. Phys. Chem. B. , vol.111 , pp. 10633-10635
    • Dehez, F.1    Tarek, M.2    Chipot, C.3
  • 117
    • 53249129575 scopus 로고    scopus 로고
    • Investigation of structures and properties of cyclic peptide nanotubes by experiment and molecular dynamics
    • Zhu, J.; Cheng, J.; Liao, Z.; Lai, Z.; Liu, B. Investigation of structures and properties of cyclic peptide nanotubes by experiment and molecular dynamics. J. Comput.-Aided Mol. Des., 2008, 22, 773-781
    • (2008) J. Comput.-Aided Mol. Des. , vol.22 , pp. 773-781
    • Zhu, J.1    Cheng, J.2    Liao, Z.3    Lai, Z.4    Liu, B.5
  • 118
    • 62249174766 scopus 로고    scopus 로고
    • Self assembly of peptides near or within membranes using coarse grained MD simulations
    • Khalfa, A.; Treptow, W.; Maigret, B.; Tarek, M. Self assembly of peptides near or within membranes using coarse grained MD simulations. Chem. Phys., 2009, 358, 161-170
    • (2009) Chem. Phys. , vol.358 , pp. 161-170
    • Khalfa, A.1    Treptow, W.2    Maigret, B.3    Tarek, M.4
  • 119
    • 77649122094 scopus 로고    scopus 로고
    • Molecular dynamics simulation for the structure of the water chain in a transmembrane peptide nanotube
    • Liu, J.; Fan, J.; Tang, M.; Zhou, W. Molecular dynamics simulation for the structure of the water chain in a transmembrane peptide nanotube. J. Phys. Chem. A., 2010, 114, 2376-2383
    • (2010) J. Phys. Chem. A. , vol.114 , pp. 2376-2383
    • Liu, J.1    Fan, J.2    Tang, M.3    Zhou, W.4
  • 120
    • 84871864524 scopus 로고    scopus 로고
    • Molecular dynamics and umbrella sampling study of stabilizing factors in cyclic peptide-based nanotubes
    • Vijayaraj, R.; Damme, S. V.; Bultinck, P.; Subramaniam, V. Molecular dynamics and umbrella sampling study of stabilizing factors in cyclic peptide-based nanotubes. J. Phys. Chem. B., 2012, 116, 9922-9933
    • (2012) J. Phys. Chem. B. , vol.116 , pp. 9922-9933
    • Vijayaraj, R.1    Damme, S.V.2    Bultinck, P.3    Subramaniam, V.4
  • 121
    • 33947221368 scopus 로고    scopus 로고
    • Molecular modeling investigation of adsorption of selfassembled peptide nanotube of cyclo-[(1R,3S)-_-Acc-D-Phe]3 in CHCl3
    • Cheng, J.; Zhu, J.; Liu, B. Molecular modeling investigation of adsorption of selfassembled peptide nanotube of cyclo-[(1R,3S)-_-Acc-D-Phe]3 in CHCl3. Chem. Phys., 2007, 333, 105-110.
    • (2007) Chem. Phys. , vol.333 , pp. 105-110
    • Cheng, J.1    Zhu, J.2    Liu, B.3
  • 122
    • 77951110595 scopus 로고    scopus 로고
    • Interaction and dimerization energies in methyl-blocked _,_-peptide nanotube segments
    • [37] García-Fandiño, R.; Castedo, L.; Granja, J.R.; Vázquez S. Interaction and dimerization energies in methyl-blocked _,_-peptide nanotube segments. J. Phys. Chem. B., 2010, 114, 4973-4983.
    • (2010) J. Phys. Chem. B. , vol.114 , pp. 4973-4983
    • García-Fandiño, R.1    Castedo, L.2    Granja, J.R.3    Vázquez, S.4
  • 124
    • 0032513708 scopus 로고    scopus 로고
    • Oriented self-assembly of cyclic peptide nanotubes in lipid membranes
    • [39] Kim, H.S.; Hartgerink, J. D.; Ghadiri, M.R. Oriented self-assembly of cyclic peptide nanotubes in lipid membranes. J.Am. Chem. Soc., 1998, 120, 4417-4424.
    • (1998) J.Am. Chem. Soc. , vol.120 , pp. 4417-4424
    • Kim, H.S.1    Hartgerink, J.D.2    Ghadiri, M.R.3
  • 127
    • 34250313965 scopus 로고    scopus 로고
    • Combinatorial approach to the discovery of biocidal sixresidue cyclic D,L-_-peptides against the bacteria methicillinresistant Staphylococcus aureus (MRSA) and
    • [43] Fletcher, J.T.; Finlay, J.A.; Callow, M.E.; Callow, J.A.; Ghadiri, M.R. A combinatorial approach to the discovery of biocidal sixresidue cyclic D,L-_-peptides against the bacteria methicillinresistant Staphylococcus aureus (MRSA) and E. coli and the Biofouling Algae Ulva linza and Navicula perminuta. Chem.–Eur. J., 2007, 13, 4008-4013.
    • (2007) Chem.–Eur. J. , vol.13 , pp. 4008-4013
    • Fletcher, J.T.1    Finlay, J.A.2    Callow, M.E.3    Callow, J.A.4    Ghadiri, M.5
  • 129
    • 42949130602 scopus 로고    scopus 로고
    • New strategies and methods in the discovery of natural product anti-infective agents: The mannopeptimycins
    • [45] Koehn, F.E. New strategies and methods in the discovery of natural product anti-infective agents: the mannopeptimycins. J. Med. Chem., 2008, 51, 2613-2617
    • (2008) J. Med. Chem. , vol.51 , pp. 2613-2617
    • Koehn, F.E.1
  • 130
    • 21344461453 scopus 로고    scopus 로고
    • Mannopeptimycins, a novel class of glycopeptide antibiotics active against gram-positive bacteria
    • He, H. Mannopeptimycins, a novel class of glycopeptide antibiotics active against gram-positive bacteria. Appl. Microbiol. Biotechnol., 2005, 67, 444-452
    • (2005) Appl. Microbiol. Biotechnol. , vol.67 , pp. 444-452
    • He, H.1
  • 134
    • 53849146070 scopus 로고    scopus 로고
    • Folding Control in Cyclic Peptides through N-Methylation Pattern Selection: Formation of Antiparallel _-Sheet Dimers, Double Reverse Turns and Supramolecular Helices by 3_,_ Cyclic Peptides
    • [49] Amorín, M.; Castedo, L.; Granja, J.R. Folding Control in Cyclic Peptides through N-Methylation Pattern Selection: Formation of Antiparallel _-Sheet Dimers, Double Reverse Turns and Supramolecular Helices by 3_,_ Cyclic Peptides. Chem.–Eur. J., 2008, 14, 2100-2111.
    • (2008) Chem.–Eur. J. , vol.14 , pp. 2100-2111
    • Amorín, M.1    Castedo, L.2    Granja, J.R.3
  • 135
    • 84868018737 scopus 로고    scopus 로고
    • Selfassembling properties of all _-cyclic peptides containing sugar amino acid residue
    • [50] Guerra, A.; Brea, R.J.; Amorín, M.; Castedo, L.; Granja, J.R. Selfassembling properties of all _-cyclic peptides containing sugar amino acid residue. Osrg. Biomol. Chem., 2012, 10, 8762-8766.
    • (2012) Osrg. Biomol. Chem. , vol.10 , pp. 8762-8766
    • Guerra, A.1    Brea, R.J.2    Amorín, M.3    Castedo, L.4    Granja, J.R.5
  • 136
    • 0347190177 scopus 로고    scopus 로고
    • Synthesis and conformational analysis of linear and cyclic peptides containing sugar amino acids
    • [51] von Roedern, E.G.; Lohof, E.; Hessler, G.; Hoffmann, M.; Kessler, H. Synthesis and conformational analysis of linear and cyclic peptides containing sugar amino acids. J. Am. Chem. Soc., 1996, 118, 10156-10157.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 10156-10157
    • Von Roedern, E.G.1    Lohof, E.2    Hessler, G.3    Hoffmann, M.4    Kessler, H.5
  • 139
    • 78649915651 scopus 로고    scopus 로고
    • Molecular Insights on the Cyclic Peptide Nanotube-Mediated Transportation of Antitumor Drug 5-Fluorouracil
    • [54] Liu, H.; Chen, J.; Shen, Q.; Fu, W.; Wu, W. Molecular Insights on the Cyclic Peptide Nanotube-Mediated Transportation of Antitumor Drug 5-Fluorouracil. Mol. Pharmaceut., 2010, 7, 1985-1994.
    • (2010) Mol. Pharmaceut. , vol.7 , pp. 1985-1994
    • Liu, H.1    Chen, J.2    Shen, Q.3    Fu, W.4    Wu, W.5
  • 140
    • 84893793731 scopus 로고    scopus 로고
    • Doxorubicin-Loaded Cyclic Peptide Nanotube Bundles Overcome Chemoresistance in Breast Cancer Cells
    • [55] Wang, Y.; Yi, S.; Sun, L.; Huang, Y.; Lenaghan, S.C.; Zhang, M. Doxorubicin-Loaded Cyclic Peptide Nanotube Bundles Overcome Chemoresistance in Breast Cancer Cells. J. Biomed. Nanotechnol., 2014, 10, 445-454.
    • (2014) J. Biomed. Nanotechnol. , vol.10 , pp. 445-454
    • Wang, Y.1    Yi, S.2    Sun, L.3    Huang, Y.4    Lenaghan, S.C.5    Zhang, M.6


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