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Volumn 44, Issue 3, 2013, Pages 821-833

Cationic membrane peptides: Atomic-level insight of structure-activity relationships from solid-state NMR

Author keywords

Antimicrobial peptides; Cationic membrane peptide; Cell penetrating peptides; Guanidinium phosphate complex; Solid state NMR

Indexed keywords

ARGININE; CATIONIC MEMBRANE PEPTIDE; CELL PENETRATING PEPTIDE; GUANIDINE; GUANIDINIUM PHOSPHATE; LYSINE; MEMBRANE PROTEIN; PHOSPHOLIPID; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG; VOLTAGE GATED POTASSIUM CHANNEL;

EID: 84878375114     PISSN: 09394451     EISSN: 14382199     Source Type: Journal    
DOI: 10.1007/s00726-012-1421-9     Document Type: Review
Times cited : (66)

References (116)
  • 1
    • 53249147452 scopus 로고    scopus 로고
    • Solution structure and model membrane interactions of temporins-SH, antimicrobial peptides from amphibian skin. A NMR spectroscopy and differential scanning calorimetery study
    • 18795798 1:CAS:528:DC%2BD1cXhtFWksL%2FF 10.1021/bi8006884
    • Abbassi F, Galanth C, Amiche M, Saito K, Piesse C, Zargarian L, Hani K, Nicolas P, Lequin O, Ladram A (2008) Solution structure and model membrane interactions of temporins-SH, antimicrobial peptides from amphibian skin. A NMR spectroscopy and differential scanning calorimetery study. Biochemistry 47:10513-10525
    • (2008) Biochemistry , vol.47 , pp. 10513-10525
    • Abbassi, F.1    Galanth, C.2    Amiche, M.3    Saito, K.4    Piesse, C.5    Zargarian, L.6    Hani, K.7    Nicolas, P.8    Lequin, O.9    Ladram, A.10
  • 2
    • 62649113057 scopus 로고    scopus 로고
    • Structural rearrangements of membrane proteins probed by water-edited solid-state NMR spectroscopy
    • 10.1021/ja806306e 1:CAS:528:DC%2BD1cXhsVOmt7rO
    • Ader C, Schneider R, Seidel K, Etzkorn M, Becker S, Baldus M (2008) Structural rearrangements of membrane proteins probed by water-edited solid-state NMR spectroscopy. J Am Chem Soc 131(1):170-176
    • (2008) J Am Chem Soc , vol.131 , Issue.1 , pp. 170-176
    • Ader, C.1    Schneider, R.2    Seidel, K.3    Etzkorn, M.4    Becker, S.5    Baldus, M.6
  • 3
    • 33847048443 scopus 로고    scopus 로고
    • Molecular dynamics simulations of a mixed DOPC/DOPG bilayer
    • 15011033 1:CAS:528:DC%2BD2cXnsVemsr8%3D 10.1140/epjed/e2003-01-031-3
    • Balali-Mood K, Harroun TA, Bradshaw JP (2003) Molecular dynamics simulations of a mixed DOPC/DOPG bilayer. Eur Phys J E 12:S135-S140
    • (2003) Eur Phys J e , vol.12
    • Balali-Mood, K.1    Harroun, T.A.2    Bradshaw, J.P.3
  • 4
    • 0016311447 scopus 로고
    • A molecular model of membrane excitability
    • 4461846 1:CAS:528:DyaE2MXksVSqsr4%3D 10.1002/jss.400020504
    • Baumann G, Mueller P (1974) A molecular model of membrane excitability. J Supramol Struct 2(5-6):538-557
    • (1974) J Supramol Struct , vol.2 , Issue.5-6 , pp. 538-557
    • Baumann, G.1    Mueller, P.2
  • 5
    • 0032717887 scopus 로고    scopus 로고
    • The structure, dynamics, and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy
    • 10590307 1:CAS:528:DyaK1MXnslylsr4%3D 10.1016/S0005-2736(99)00205-9
    • Bechinger B (1999) The structure, dynamics, and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy. Biochim Biophys Acta 1462:157-183
    • (1999) Biochim Biophys Acta , vol.1462 , pp. 157-183
    • Bechinger, B.1
  • 6
    • 0029757155 scopus 로고    scopus 로고
    • Binding of small basic peptides to membranes containing acidic lipids: Theoretical models and experimental results
    • 8842196 1:CAS:528:DyaK28XkslOqtL4%3D 10.1016/S0006-3495(96)79280-9
    • Ben-Tal N, Honig B, Peitzsch RM, Denisov G, McLaughlin S (1996) Binding of small basic peptides to membranes containing acidic lipids: theoretical models and experimental results. Biophys J 71:561-575
    • (1996) Biophys J , vol.71 , pp. 561-575
    • Ben-Tal, N.1    Honig, B.2    Peitzsch, R.M.3    Denisov, G.4    McLaughlin, S.5
  • 7
    • 79960607694 scopus 로고    scopus 로고
    • Solid-state NMR of proteins sedimented by ultracentrifugation
    • 21670262 1:CAS:528:DC%2BC3MXovFentrg%3D 10.1073/pnas.1103854108
    • Bertini I, Luchinat C, Parigi G, Ravera E, Reif B, Turano P (2011) Solid-state NMR of proteins sedimented by ultracentrifugation. Proc Natl Acad Sci USA 108(26):10396-10399
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.26 , pp. 10396-10399
    • Bertini, I.1    Luchinat, C.2    Parigi, G.3    Ravera, E.4    Reif, B.5    Turano, P.6
  • 8
    • 0041843710 scopus 로고    scopus 로고
    • Charge-dependent translocation of the Trojan peptide penetratin across lipid membranes
    • 12885645 1:CAS:528:DC%2BD3sXmtVyks74%3D 10.1016/S0006-3495(03)74537-8
    • Binder H, Lindblom G (2003) Charge-dependent translocation of the Trojan peptide penetratin across lipid membranes. Biophys J 85:982-995
    • (2003) Biophys J , vol.85 , pp. 982-995
    • Binder, H.1    Lindblom, G.2
  • 9
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?
    • 15703760 1:CAS:528:DC%2BD2MXhslGjtbo%3D 10.1038/nrmicro1098
    • Brogden KA (2005) Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat Rev Microbiol 3(3):238-250
    • (2005) Nat Rev Microbiol , vol.3 , Issue.3 , pp. 238-250
    • Brogden, K.A.1
  • 10
    • 0345276804 scopus 로고    scopus 로고
    • Immobilization and aggregation of the antimicrobial peptide protegrin-1 in lipid bilayers investigated by solid-state NMR
    • 14622019 1:CAS:528:DC%2BD3sXosFKiu7w%3D 10.1021/bi035187w
    • Buffy JJ, Waring AJ, Lehrer RI, Hong M (2003) Immobilization and aggregation of the antimicrobial peptide protegrin-1 in lipid bilayers investigated by solid-state NMR. Biochemistry 42(46):13725-13734
    • (2003) Biochemistry , vol.42 , Issue.46 , pp. 13725-13734
    • Buffy, J.J.1    Waring, A.J.2    Lehrer, R.I.3    Hong, M.4
  • 11
    • 3342900055 scopus 로고    scopus 로고
    • Solid-state NMR investigation of the selective perturbation of lipid bilayers by the cyclic antimicrobial peptide RTD-1
    • 15274634 1:CAS:528:DC%2BD2cXlsVelsbw%3D 10.1021/bi036243w
    • Buffy JJ, McCormick MJ, Wi S, Waring A, Lehrer RI, Hong M (2004) Solid-state NMR investigation of the selective perturbation of lipid bilayers by the cyclic antimicrobial peptide RTD-1. Biochemistry 43:9800-9812
    • (2004) Biochemistry , vol.43 , pp. 9800-9812
    • Buffy, J.J.1    McCormick, M.J.2    Wi, S.3    Waring, A.4    Lehrer, R.I.5    Hong, M.6
  • 12
    • 0026350074 scopus 로고
    • Arginine-mediated RNA recognition: The arginine fork
    • 1:CAS:528:DyaK3MXlslOku7w%3D 10.1126/science.252.5009.1167
    • Calnan BJ, Tidor B, Biancalana S, Hudson D, Frankel AD (1991) Arginine-mediated RNA recognition: the arginine fork. Science 252(5010):1167-1171
    • (1991) Science , vol.252 , Issue.5010 , pp. 1167-1171
    • Calnan, B.J.1    Tidor, B.2    Biancalana, S.3    Hudson, D.4    Frankel, A.D.5
  • 13
    • 33748988741 scopus 로고    scopus 로고
    • Tryptophan- and arginine-rich antimicrobial peptides: Structures and mechanisms of action
    • 16756942 1:CAS:528:DC%2BD28XhtVanu7rP 10.1016/j.bbamem.2006.04.006
    • Chan DI, Prenner EJ, Vogel HJ (2006) Tryptophan- and arginine-rich antimicrobial peptides: structures and mechanisms of action. Biochim Biophys Acta 1758:1184-1202
    • (2006) Biochim Biophys Acta , vol.1758 , pp. 1184-1202
    • Chan, D.I.1    Prenner, E.J.2    Vogel, H.J.3
  • 14
    • 0033858613 scopus 로고    scopus 로고
    • Development of protegrins for the treatment and prevention of oral mucositis: Structure-activity relationships of synthetic protegrin analogues
    • 10931444 1:CAS:528:DC%2BD3cXmsVyls78%3D 10.1002/1097-0282(2000)55: 1<88: AID-BIP80>3.0.CO;2-K
    • Chen J, Falla TJ, Liu H, Hurst MA, Fujii CA, Mosca DA, Embree JR, Loury DJ, Radel PA, Cheng CC, Gu L, Fiddes JC (2000) Development of protegrins for the treatment and prevention of oral mucositis: structure-activity relationships of synthetic protegrin analogues. Biopolymers 55:88-98
    • (2000) Biopolymers , vol.55 , pp. 88-98
    • Chen, J.1    Falla, T.J.2    Liu, H.3    Hurst, M.A.4    Fujii, C.A.5    Mosca, D.A.6    Embree, J.R.7    Loury, D.J.8    Radel, P.A.9    Cheng, C.C.10    Gu, L.11    Fiddes, J.C.12
  • 16
    • 0035919725 scopus 로고    scopus 로고
    • Optimization of the antimicrobial activity of magainin peptides by modification of charge
    • 11470274 1:CAS:528:DC%2BD3MXltlKqtbo%3D 10.1016/S0014-5793(01)02648-5
    • Dathe M, Nikolenko H, Meyer J, Beyermann M, Bienert M (2001) Optimization of the antimicrobial activity of magainin peptides by modification of charge. FEBS Lett 501(2-3):146-150
    • (2001) FEBS Lett , vol.501 , Issue.2-3 , pp. 146-150
    • Dathe, M.1    Nikolenko, H.2    Meyer, J.3    Beyermann, M.4    Bienert, M.5
  • 17
    • 0028188303 scopus 로고
    • Chemical shifts of carbonyl carbons in peptides and proteins
    • De Dios AC, Oldfield E (1994) Chemical shifts of carbonyl carbons in peptides and proteins. J Am Chem Soc 116:11485-11488
    • (1994) J Am Chem Soc , vol.116 , pp. 11485-11488
    • De Dios, A.C.1    Oldfield, E.2
  • 18
    • 84859917360 scopus 로고    scopus 로고
    • Dipolar recoupling in magic angle spinning solid-state nuclear magnetic resonance
    • 22404583 10.1146/annurev-physchem-032511-143726 1:CAS:528: DC%2BC38Xnt1GksL4%3D
    • De Paëpe G (2012) Dipolar recoupling in magic angle spinning solid-state nuclear magnetic resonance. Annu Rev Phys Chem 63:661-684
    • (2012) Annu Rev Phys Chem , vol.63 , pp. 661-684
    • De Paëpe, G.1
  • 19
    • 0028239908 scopus 로고
    • The third helix of the Antennapedia homeodomain translocates through biological membranes
    • 8144628 1:CAS:528:DyaK2cXlt1Oqt7Y%3D
    • Derossi D, Joliot AH, Chassaing G, Prochiantz A (1994) The third helix of the Antennapedia homeodomain translocates through biological membranes. J Biol Chem 269:10444-10450
    • (1994) J Biol Chem , vol.269 , pp. 10444-10450
    • Derossi, D.1    Joliot, A.H.2    Chassaing, G.3    Prochiantz, A.4
  • 20
    • 0031984072 scopus 로고    scopus 로고
    • Trojan peptides: The penetratin system for intracellular delivery
    • 9695814 1:CAS:528:DyaK1cXhtlSlt74%3D
    • Derossi D, Chassaing G, Prochiantz A (1998) Trojan peptides: the penetratin system for intracellular delivery. Trends Cell Biol 8(2):84-87
    • (1998) Trends Cell Biol , vol.8 , Issue.2 , pp. 84-87
    • Derossi, D.1    Chassaing, G.2    Prochiantz, A.3
  • 22
    • 33750692000 scopus 로고    scopus 로고
    • Membrane-bound conformation and topology of the antimicrobial peptide tachyplesin i by solid-state NMR
    • 17073453 1:CAS:528:DC%2BD28XhtVOqsLjI 10.1021/bi061424u
    • Doherty T, Waring AJ, Hong M (2006a) Membrane-bound conformation and topology of the antimicrobial peptide tachyplesin I by solid-state NMR. Biochemistry 45:13323-13330
    • (2006) Biochemistry , vol.45 , pp. 13323-13330
    • Doherty, T.1    Waring, A.J.2    Hong, M.3
  • 23
    • 33749058274 scopus 로고    scopus 로고
    • Peptide-lipid interactions of the beta-hairpin antimicrobial peptide tachyplesin and its linear derivatives from solid-state NMR
    • 16678119 1:CAS:528:DC%2BD28XhtVanu7jM 10.1016/j.bbamem.2006.03.016
    • Doherty T, Waring AJ, Hong M (2006b) Peptide-lipid interactions of the beta-hairpin antimicrobial peptide tachyplesin and its linear derivatives from solid-state NMR. Biochim Biophys Acta 1758:1285-1291
    • (2006) Biochim Biophys Acta , vol.1758 , pp. 1285-1291
    • Doherty, T.1    Waring, A.J.2    Hong, M.3
  • 24
    • 77955330334 scopus 로고    scopus 로고
    • High-resolution orientation and depth of insertion of the voltage-sensing S4 helix of a potassium channel in lipid bilayers
    • 1:CAS:528:DC%2BC3cXpvFWitLw%3D 10.1016/j.jmb.2010.06.048
    • Doherty T, Su Y, Hong M (2010) High-resolution orientation and depth of insertion of the voltage-sensing S4 helix of a potassium channel in lipid bilayers. J Mol Bio 401(4):642-652
    • (2010) J Mol Bio , vol.401 , Issue.4 , pp. 642-652
    • Doherty, T.1    Su, Y.2    Hong, M.3
  • 25
    • 34247633528 scopus 로고    scopus 로고
    • On the thermodynamic stability of a charged arginine side chain in a transmembrane helix
    • 17360368 1:CAS:528:DC%2BD2sXjvFKitbY%3D 10.1073/pnas.0610470104
    • Dorairaj S, Allen TW (2007) On the thermodynamic stability of a charged arginine side chain in a transmembrane helix. Proc Natl Acad Sci USA 104(12):4943-4948
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.12 , pp. 4943-4948
    • Dorairaj, S.1    Allen, T.W.2
  • 26
    • 0032717048 scopus 로고    scopus 로고
    • Diversity of antimicrobial peptides and their mechanisms of action
    • 10590300 1:CAS:528:DyaK1MXnslymurg%3D 10.1016/S0005-2736(99)00198-4
    • Epand RM, Vogel HJ (1999) Diversity of antimicrobial peptides and their mechanisms of action. Biochim Biophys Acta 1462:11-28
    • (1999) Biochim Biophys Acta , vol.1462 , pp. 11-28
    • Epand, R.M.1    Vogel, H.J.2
  • 27
    • 0030198873 scopus 로고    scopus 로고
    • Solution structure of protegrin-1, a broad-spectrum antimicrobial peptide from porcine leukocytes
    • 8807886 1:CAS:528:DyaK28XkvFWgurg%3D 10.1016/S1074-5521(96)90145-3
    • Fahrner RL, Dieckmann T, Harwig SS, Lehrer RI, Eisenberg D, Feigon J (1996) Solution structure of protegrin-1, a broad-spectrum antimicrobial peptide from porcine leukocytes. Chem Biol 3:543-550
    • (1996) Chem Biol , vol.3 , pp. 543-550
    • Fahrner, R.L.1    Dieckmann, T.2    Harwig, S.S.3    Lehrer, R.I.4    Eisenberg, D.5    Feigon, J.6
  • 28
    • 12444303255 scopus 로고    scopus 로고
    • Highly efficient, nonpeptidic oligo-guanidinium vectors that selectively internalize into mitochondria
    • 15656624 1:CAS:528:DC%2BD2MXkvVOmsA%3D%3D 10.1021/ja044006q
    • Fernandez-Carneado J, Van Gool M, Martos V, Castel S, Prados P, De Mendoza J, Giralt E (2005) Highly efficient, nonpeptidic oligo-guanidinium vectors that selectively internalize into mitochondria. J Am Chem Soc 127:869-874
    • (2005) J Am Chem Soc , vol.127 , pp. 869-874
    • Fernandez-Carneado, J.1    Van Gool, M.2    Martos, V.3    Castel, S.4    Prados, P.5    De Mendoza, J.6    Giralt, E.7
  • 29
    • 31544438701 scopus 로고    scopus 로고
    • Break on through to the other side-biophysics and cell biology shed light on cell-penetrating peptides
    • 16254940 1:CAS:528:DC%2BD2MXhtlalu7bO 10.1002/cbic.200500044
    • Fischer R, Fotin-Mleczek M, Hufnagel H, Brock R (2005) Break on through to the other side-biophysics and cell biology shed light on cell-penetrating peptides. ChemBioChem 6:2126-2142
    • (2005) ChemBioChem , vol.6 , pp. 2126-2142
    • Fischer, R.1    Fotin-Mleczek, M.2    Hufnagel, H.3    Brock, R.4
  • 30
    • 0024262589 scopus 로고
    • Cellular uptake of the TAT protein from human lmmunodeficiency virus
    • 2849510 1:CAS:528:DyaL1MXlsFOnsA%3D%3D 10.1016/0092-8674(88)90263-2
    • Frankel AD, Pabo CO (1988) Cellular uptake of the TAT protein from human lmmunodeficiency virus. Cell 55:1189-1193
    • (1988) Cell , vol.55 , pp. 1189-1193
    • Frankel, A.D.1    Pabo, C.O.2
  • 31
    • 27244444569 scopus 로고    scopus 로고
    • Interface connections of a transmembrane voltage sensor
    • 16217012 1:CAS:528:DC%2BD2MXhtFGqtb%2FF 10.1073/pnas.0507618102
    • Freites JA, Tobias DJ, von Heijne G, White SH (2005) Interface connections of a transmembrane voltage sensor. Proc Natl Acad Sci USA 102(42):15059-15064
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.42 , pp. 15059-15064
    • Freites, J.A.1    Tobias, D.J.2    Von Heijne, G.3    White, S.H.4
  • 32
    • 0035937124 scopus 로고    scopus 로고
    • Arginine-rich peptides. An abundant source of membrane-permeable peptides having potential as carriers for intracellular protein delivery
    • 11084031 1:CAS:528:DC%2BD3MXhs1KmtL0%3D 10.1074/jbc.M007540200
    • Futaki S, Suzuki T, Ohashi W, Yagami T, Tanaka S, Ueda K, Sugiura Y (2001) Arginine-rich peptides. An abundant source of membrane-permeable peptides having potential as carriers for intracellular protein delivery. J Biol Chem 276(8):5836-5840
    • (2001) J Biol Chem , vol.276 , Issue.8 , pp. 5836-5840
    • Futaki, S.1    Suzuki, T.2    Ohashi, W.3    Yagami, T.4    Tanaka, S.5    Ueda, K.6    Sugiura, Y.7
  • 33
    • 26644469527 scopus 로고    scopus 로고
    • Basis for selectivity of cationic antimicrobial peptides for bacterial versus mammalian membranes
    • 16043484 1:CAS:528:DC%2BD2MXhtVKisbnF 10.1074/jbc.M507042200
    • Glukhov E, Stark M, Burrows LL, Deber CM (2005) Basis for selectivity of cationic antimicrobial peptides for bacterial versus mammalian membranes. J Biol Chem 280(40):33960-33967
    • (2005) J Biol Chem , vol.280 , Issue.40 , pp. 33960-33967
    • Glukhov, E.1    Stark, M.2    Burrows, L.L.3    Deber, C.M.4
  • 34
    • 0037349932 scopus 로고    scopus 로고
    • Cell-permeable peptides improve cellular uptake and therapeutic gene delivery of replication-deficient viruses in cells and in vivo
    • 12598894 1:CAS:528:DC%2BD3sXhsFGgsLs%3D 10.1038/nm835
    • Gratton J-P, Yu J, Griffith JW, Babbitt RW, Scotland RS, Hickey R, Giordano FJ, Sessa WC (2003) Cell-permeable peptides improve cellular uptake and therapeutic gene delivery of replication-deficient viruses in cells and in vivo. Nat Med 9:357-362
    • (2003) Nat Med , vol.9 , pp. 357-362
    • Gratton, J.-P.1    Yu, J.2    Griffith, J.W.3    Babbitt, R.W.4    Scotland, R.S.5    Hickey, R.6    Giordano, F.J.7    Sessa, W.C.8
  • 35
    • 0024209811 scopus 로고
    • Autonomous functional domains of chemically synthesized human immunodeficiency virus TAT trans-activator protein
    • 2849509 1:CAS:528:DyaL1MXhtlSksr0%3D 10.1016/0092-8674(88)90262-0
    • Green M, Loewenstein PM (1988) Autonomous functional domains of chemically synthesized human immunodeficiency virus TAT trans-activator protein. Cell 55(6):1179-1188
    • (1988) Cell , vol.55 , Issue.6 , pp. 1179-1188
    • Green, M.1    Loewenstein, P.M.2
  • 36
    • 45149145322 scopus 로고
    • Rotational-echo doubleresonance NMR
    • 1:CAS:528:DyaL1MXkvV2hsr8%3D
    • Gullion T, Schaefer J (1989) Rotational-echo doubleresonance NMR. J Magn Reson 81:196-200
    • (1989) J Magn Reson , vol.81 , pp. 196-200
    • Gullion, T.1    Schaefer, J.2
  • 37
    • 84859435892 scopus 로고    scopus 로고
    • Effects of the TAT peptide orientation and relative location on the protein transduction efficiency
    • 22188730 1:CAS:528:DC%2BC38Xlslagu7c%3D 10.1111/j.1747-0285.2011.01315.x
    • Guo Q, Zhao G, Hao F, Guan Y (2012) Effects of the TAT peptide orientation and relative location on the protein transduction efficiency. Chem Biol Drug Des 79(5):683-690
    • (2012) Chem Biol Drug des , vol.79 , Issue.5 , pp. 683-690
    • Guo, Q.1    Zhao, G.2    Hao, F.3    Guan, Y.4
  • 38
    • 0033596316 scopus 로고    scopus 로고
    • Surface recognition and helix stabilization of a tetraaspartate peptide by shape and electrostatic complementarity of an artificial receptor
    • 1:CAS:528:DyaK1MXnslWitrw%3D 10.1021/ja9910154
    • Haack T, Peczuh MW, Salvatella X, Sanchez-Quesada J, de Mendoza J, Hamilton AD, Giralt E (1999) Surface recognition and helix stabilization of a tetraaspartate peptide by shape and electrostatic complementarity of an artificial receptor. J Am Chem Soc 121:11813-11820
    • (1999) J Am Chem Soc , vol.121 , pp. 11813-11820
    • Haack, T.1    Peczuh, M.W.2    Salvatella, X.3    Sanchez-Quesada, J.4    De Mendoza, J.5    Hamilton, A.D.6    Giralt, E.7
  • 39
    • 38049156027 scopus 로고    scopus 로고
    • Molecular dynamics simulations suggest a mechanism for translocation of the HIV-1 TAT peptide across lipid membranes
    • 18093956 1:CAS:528:DC%2BD1cXks1yjug%3D%3D 10.1073/pnas.0706574105
    • Herce HD, Garcia AE (2007) Molecular dynamics simulations suggest a mechanism for translocation of the HIV-1 TAT peptide across lipid membranes. Proc Natl Acad Sci USA 104(52):20805-20810
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.52 , pp. 20805-20810
    • Herce, H.D.1    Garcia, A.E.2
  • 40
    • 0032590227 scopus 로고    scopus 로고
    • Resonance assignment of 13C/15N labeled proteins by two- and three-dimensional magic-angle-spinning NMR
    • 10549131 1:CAS:528:DyaK1MXntFSgsbs%3D 10.1023/A:1008334204412
    • Hong M (1999) Resonance assignment of 13C/15N labeled proteins by two- and three-dimensional magic-angle-spinning NMR. J Biomol NMR 15:1-14
    • (1999) J Biomol NMR , vol.15 , pp. 1-14
    • Hong, M.1
  • 41
    • 33845217043 scopus 로고    scopus 로고
    • Oligomeric structure, dynamics, and orientation, of membrane proteins from solid-state NMR
    • 17161364 1:CAS:528:DC%2BD28XhtlShsrvM 10.1016/j.str.2006.10.002
    • Hong M (2006) Oligomeric structure, dynamics, and orientation, of membrane proteins from solid-state NMR. Structure 14:1731-1740
    • (2006) Structure , vol.14 , pp. 1731-1740
    • Hong, M.1
  • 42
    • 79953186604 scopus 로고    scopus 로고
    • Structure and dynamics of cationic membrane peptides and proteins: Insights from solid-state NMR
    • 21344534 1:CAS:528:DC%2BC3MXjvFWmsr0%3D 10.1002/pro.600
    • Hong M, Su Y (2011) Structure and dynamics of cationic membrane peptides and proteins: insights from solid-state NMR. Protein Sci 20(4):641-655
    • (2011) Protein Sci , vol.20 , Issue.4 , pp. 641-655
    • Hong, M.1    Su, Y.2
  • 43
    • 84866359064 scopus 로고    scopus 로고
    • Hydrogen-bonding partner of the proton-conducting histidine in the influenza m2 proton channel revealed from 1h chemical shifts
    • Hong M, Fritzsching KJ, Williams JK (2012a) Hydrogen-bonding partner of the proton-conducting histidine in the influenza m2 proton channel revealed from 1h chemical shifts. J Am Chem Soc 134:14753-14755
    • (2012) J Am Chem Soc , vol.134 , pp. 14753-14755
    • Hong, M.1    Fritzsching, K.J.2    Williams, J.K.3
  • 44
    • 84859912916 scopus 로고    scopus 로고
    • Membrane protein structure and dynamics from NMR spectroscopy
    • 22136620 1:CAS:528:DC%2BC38Xnt1GltLY%3D 10.1146/annurev-physchem-032511- 143731
    • Hong M, Zhang Y, Hu F (2012b) Membrane protein structure and dynamics from NMR spectroscopy. Annu Rev Phys Chem 63:1-24
    • (2012) Annu Rev Phys Chem , vol.63 , pp. 1-24
    • Hong, M.1    Zhang, Y.2    Hu, F.3
  • 45
    • 74849099434 scopus 로고    scopus 로고
    • Detection of a transient intermediate in a rapid protein folding process by solid-state nuclear magnetic resonance
    • 20000466 1:CAS:528:DC%2BD1MXhsFClsbfF 10.1021/ja908471n
    • Hu KN, Yau WM, Tycko R (2010) Detection of a transient intermediate in a rapid protein folding process by solid-state nuclear magnetic resonance. J Am Chem Soc 132(1):24-25
    • (2010) J Am Chem Soc , vol.132 , Issue.1 , pp. 24-25
    • Hu, K.N.1    Yau, W.M.2    Tycko, R.3
  • 46
    • 0037028547 scopus 로고    scopus 로고
    • Membrane protein topology probed by H-1 spin diffusion from lipids using solid-state NMR spectroscopy
    • 11817963 1:CAS:528:DC%2BD38Xit1OjtA%3D%3D 10.1021/ja017001r
    • Huster D, Yao XL, Hong M (2002) Membrane protein topology probed by H-1 spin diffusion from lipids using solid-state NMR spectroscopy. J Am Chem Soc 124(5):874-883
    • (2002) J Am Chem Soc , vol.124 , Issue.5 , pp. 874-883
    • Huster, D.1    Yao, X.L.2    Hong, M.3
  • 47
    • 0034830333 scopus 로고    scopus 로고
    • Frequency selective heteronuclear dipolar recoupling in rotating solids: Accurate 13C-15N distance measurements in uniformly 13C,15N-labeled peptides
    • 11472123 1:CAS:528:DC%2BD3MXhvFGrtLw%3D 10.1021/ja003266e
    • Jaroniec CP, Tounge BA, Herzfeld J, Griffin RG (2001) Frequency selective heteronuclear dipolar recoupling in rotating solids: accurate 13C-15N distance measurements in uniformly 13C,15N-labeled peptides. J Am Chem Soc 123:3507-3519
    • (2001) J Am Chem Soc , vol.123 , pp. 3507-3519
    • Jaroniec, C.P.1    Tounge, B.A.2    Herzfeld, J.3    Griffin, R.G.4
  • 48
    • 84864065351 scopus 로고    scopus 로고
    • Membrane adsorption and binding, cellular uptake and cytotoxicity of cell-penetrating peptidomimetics with α-peptide/β-peptoid backbone: Effects of hydrogen bonding and α-chirality in the β-peptoid residues
    • 22609348 1:CAS:528:DC%2BC38Xht1emt7bM 10.1016/j.bbamem.2012.05.003
    • Jing X, Yang M, Kasimova MR, Malmsten M, Franzyk H, Jorgensen L, Foged C, Nielsen HM (2012) Membrane adsorption and binding, cellular uptake and cytotoxicity of cell-penetrating peptidomimetics with α-peptide/β- peptoid backbone: effects of hydrogen bonding and α-chirality in the β-peptoid residues. Biochim Biophys Acta 1818(11):2660-2668
    • (2012) Biochim Biophys Acta , vol.1818 , Issue.11 , pp. 2660-2668
    • Jing, X.1    Yang, M.2    Kasimova, M.R.3    Malmsten, M.4    Franzyk, H.5    Jorgensen, L.6    Foged, C.7    Nielsen, H.M.8
  • 49
    • 57349182296 scopus 로고    scopus 로고
    • Effect of cell-penetrating peptides on the nasal absorption of insulin
    • 10.1016/j.jconrel.2008.09.076 1:CAS:528:DC%2BD1cXhsV2hsrrO
    • Khafagya E-S, Morishitaa M, Isowab K, Imaib J, Takayamaa K (2009) Effect of cell-penetrating peptides on the nasal absorption of insulin. J Contolled Release 133(2):103-108
    • (2009) J Contolled Release , vol.133 , Issue.2 , pp. 103-108
    • Khafagya, E.-S.1    Morishitaa, M.2    Isowab, K.3    Imaib, J.4    Takayamaa, K.5
  • 50
    • 0141942111 scopus 로고    scopus 로고
    • Membrane translocation of penetratin and its derivatives in different cell lines
    • 14523940 1:CAS:528:DC%2BD3sXotFOmsr4%3D 10.1002/jmr.637
    • Letoha T, Gaál S, Somlai C, Czajlik A, Perczel A, Penke B (2003) Membrane translocation of penetratin and its derivatives in different cell lines. J Mol Recognit 16:272-279
    • (2003) J Mol Recognit , vol.16 , pp. 272-279
    • Letoha, T.1    Gaál, S.2    Somlai, C.3    Czajlik, A.4    Perczel, A.5    Penke, B.6
  • 51
    • 79551714030 scopus 로고    scopus 로고
    • Protonation, tautomerization, and rotameric structure of histidine: A comprehensive study by magic-angle-spinning solid-state NMR
    • 21207964 1:CAS:528:DC%2BC3MXit1equw%3D%3D 10.1021/ja108943n
    • Li S, Hong M (2011) Protonation, tautomerization, and rotameric structure of histidine: a comprehensive study by magic-angle-spinning solid-state NMR. J Am Chem Soc 133(5):1534-1544
    • (2011) J Am Chem Soc , vol.133 , Issue.5 , pp. 1534-1544
    • Li, S.1    Hong, M.2
  • 52
    • 50549085702 scopus 로고    scopus 로고
    • Potential of mean force and pKa profile calculation for a lipid membrane-exposed arginine side chain
    • 18636765 1:CAS:528:DC%2BD1cXos1ahtrw%3D 10.1021/jp7114912
    • Li L, Vorobyov I, Allen TW (2008) Potential of mean force and pKa profile calculation for a lipid membrane-exposed arginine side chain. J Phys Chem B 112(32):9574-9587
    • (2008) J Phys Chem B , vol.112 , Issue.32 , pp. 9574-9587
    • Li, L.1    Vorobyov, I.2    Allen, T.W.3
  • 53
    • 77949795332 scopus 로고    scopus 로고
    • Water-protein interactions of an arginine-rich membrane peptide in lipid bilayers investigated by solid-state nuclear magnetic resonance spectroscopy
    • 20199036 1:CAS:528:DC%2BC3cXislKht78%3D 10.1021/jp912283r
    • Li S, Su Y, Luo W, Hong M (2010) Water-protein interactions of an arginine-rich membrane peptide in lipid bilayers investigated by solid-state nuclear magnetic resonance spectroscopy. J Phys Chem B 114(11):4063-4069
    • (2010) J Phys Chem B , vol.114 , Issue.11 , pp. 4063-4069
    • Li, S.1    Su, Y.2    Luo, W.3    Hong, M.4
  • 56
    • 77749267718 scopus 로고    scopus 로고
    • Conformational changes of an ion channel detected through water-protein interactions using solid-state NMR spectroscopy
    • 20112896 1:CAS:528:DC%2BC3cXht1Knu7k%3D 10.1021/ja9096219
    • Luo W, Hong M (2010) Conformational changes of an ion channel detected through water-protein interactions using solid-state NMR spectroscopy. J Am Chem Soc 132(7):2378-2384
    • (2010) J Am Chem Soc , vol.132 , Issue.7 , pp. 2378-2384
    • Luo, W.1    Hong, M.2
  • 58
    • 0034106918 scopus 로고    scopus 로고
    • Structure-function relationships of temporins, small antimicrobial peptides from amphibian skin
    • 10691983 1:CAS:528:DC%2BD3cXhvVagsL8%3D 10.1046/j.1432-1327.2000.01143.x
    • Mangoni ML, Rinaldi AC, Di Giulio A, Mignogna D, Bozzi A, Barra D, Simmaco M (2000) Structure-function relationships of temporins, small antimicrobial peptides from amphibian skin. Eur J Biochem 267:1447-1454
    • (2000) Eur J Biochem , vol.267 , pp. 1447-1454
    • Mangoni, M.L.1    Rinaldi, A.C.2    Di Giulio, A.3    Mignogna, D.4    Bozzi, A.5    Barra, D.6    Simmaco, M.7
  • 59
    • 33750820630 scopus 로고    scopus 로고
    • Membrane-dependent oligomeric structure and pore formation of a b-hairpin antimicrobial peptide in lipid bilayers from solid-state NMR
    • 17060626 1:CAS:528:DC%2BD28Xht1WmsL3I 10.1073/pnas.0605079103
    • Mani R, Cady SD, Tang M, Waring AJ, Lehrer RI, Hong M (2006) Membrane-dependent oligomeric structure and pore formation of a b-hairpin antimicrobial peptide in lipid bilayers from solid-state NMR. Proc Natl Acad Sci USA 103:16242-16247
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 16242-16247
    • Mani, R.1    Cady, S.D.2    Tang, M.3    Waring, A.J.4    Lehrer, R.I.5    Hong, M.6
  • 60
    • 0032693639 scopus 로고    scopus 로고
    • Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes
    • 10590299 1:CAS:528:DyaK1MXnslymuro%3D
    • Matsuzaki K (1999) Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes. Biochim Biophys Acta 1462(1-2):1-10
    • (1999) Biochim Biophys Acta , vol.1462 , Issue.1-2 , pp. 1-10
    • Matsuzaki, K.1
  • 61
    • 0028208901 scopus 로고
    • Orientational and aggregational states of magainin 2 in phospholipid bilayers
    • 8136371 1:CAS:528:DyaK2cXhvVans7k%3D 10.1021/bi00177a027
    • Matsuzaki K, Murase O, Tokuda H, Funakoshi S, Fujii N, Miyajima K (1994) Orientational and aggregational states of magainin 2 in phospholipid bilayers. Biochemistry 33:3342-3349
    • (1994) Biochemistry , vol.33 , pp. 3342-3349
    • Matsuzaki, K.1    Murase, O.2    Tokuda, H.3    Funakoshi, S.4    Fujii, N.5    Miyajima, K.6
  • 62
    • 67650285019 scopus 로고    scopus 로고
    • Structure and dynamics of membrane proteins by magic angle spinning solid-state NMR
    • 19245337 1:CAS:528:DC%2BD1MXntlentb0%3D 10.1146/annurev.biophys.050708. 133719
    • McDermott AE (2009) Structure and dynamics of membrane proteins by magic angle spinning solid-state NMR. Annu Rev Biophys 38:385-403
    • (2009) Annu Rev Biophys , vol.38 , pp. 385-403
    • McDermott, A.E.1
  • 63
    • 0033794501 scopus 로고    scopus 로고
    • Polyarginine enters cells more efficiently than other polycationic homopolymers
    • 11095185 1:CAS:528:DC%2BD3cXnvVGltbY%3D 10.1034/j.1399-3011.2000.00723.x
    • Mitchell DJ, Steinman L, Kim DT, Fathman CG, Rothbard JB (2000) Polyarginine enters cells more efficiently than other polycationic homopolymers. J Pept Res 56(5):318-325
    • (2000) J Pept Res , vol.56 , Issue.5 , pp. 318-325
    • Mitchell, D.J.1    Steinman, L.2    Kim, D.T.3    Fathman, C.G.4    Rothbard, J.B.5
  • 64
    • 0035860429 scopus 로고    scopus 로고
    • Penetratin-induced aggregation and subsequent dissociation of negatively charged phospholipid vesicles
    • 11566195 1:CAS:528:DC%2BD3MXmvVylt7g%3D 10.1016/S0014-5793(01)02843-5
    • Persson D, Thorén PE, Nordén B (2001) Penetratin-induced aggregation and subsequent dissociation of negatively charged phospholipid vesicles. FEBS Lett 505(2):307
    • (2001) FEBS Lett , vol.505 , Issue.2 , pp. 307
    • Persson, D.1    Thorén, P.E.2    Nordén, B.3
  • 65
    • 78149426499 scopus 로고    scopus 로고
    • Solid-state NMR spectroscopy of complex molecules
    • 10.1002/anie.201002823 1:CAS:528:DC%2BC3cXhtlGmsrjF
    • Renault M, Cukkemane A, Baldus M (2011) Solid-state NMR spectroscopy of complex molecules. Angew Chem Int Ed 49:8346-8357
    • (2011) Angew Chem Int Ed , vol.49 , pp. 8346-8357
    • Renault, M.1    Cukkemane, A.2    Baldus, M.3
  • 67
    • 0034623539 scopus 로고    scopus 로고
    • 2D and 3D 15N-13C-13C NMR chemical shift correlation spectroscopy of solids: Assignment of MAS spectra of peptides
    • 1:CAS:528:DC%2BD3cXnsVKnsrc%3D 10.1021/ja001092v
    • Rienstra CM, Hohwy M, Hong M (2000) 2D and 3D 15N-13C-13C NMR chemical shift correlation spectroscopy of solids: assignment of MAS spectra of peptides. J Am Chem Soc 122:10979-10990
    • (2000) J Am Chem Soc , vol.122 , pp. 10979-10990
    • Rienstra, C.M.1    Hohwy, M.2    Hong, M.3
  • 68
    • 78549281427 scopus 로고    scopus 로고
    • Spectroscopy: Clear signals from surfaces
    • Robert GG (2010) Spectroscopy: Clear signals from surfaces. Nature 468:381-382
    • (2010) Nature , vol.468 , pp. 381-382
    • Robert, G.G.1
  • 69
    • 13844272403 scopus 로고    scopus 로고
    • Adaptive translocation: The role of hydrogen bonding and membrane potential in the uptake of guanidinium-rich transporters into cells
    • 15722160 1:CAS:528:DC%2BD2MXhslWgu7g%3D 10.1016/j.addr.2004.10.003
    • Rothbard JB, Jessop TC, Wender PA (2005) Adaptive translocation: the role of hydrogen bonding and membrane potential in the uptake of guanidinium-rich transporters into cells. Adv Drug Deliv Rev 57(4):495
    • (2005) Adv Drug Deliv Rev , vol.57 , Issue.4 , pp. 495
    • Rothbard, J.B.1    Jessop, T.C.2    Wender, P.A.3
  • 70
    • 0032536098 scopus 로고    scopus 로고
    • Oligomerization of protegrin-1 in the presence of DPC micelles. A proton high-resolution NMR study
    • 9468319 1:CAS:528:DyaK1cXislygtw%3D%3D 10.1016/S0014-5793(97)01579-2
    • Roumestand C, Louis V, Aumelas A, Grassy G, Calas B, Chavanieu A (1998) Oligomerization of protegrin-1 in the presence of DPC micelles. A proton high-resolution NMR study. FEBS Lett 421:263-267
    • (1998) FEBS Lett , vol.421 , pp. 263-267
    • Roumestand, C.1    Louis, V.2    Aumelas, A.3    Grassy, G.4    Calas, B.5    Chavanieu, A.6
  • 72
    • 0038911680 scopus 로고    scopus 로고
    • Anion helicates: Double strand helical self-assembly of chiral bicyclic guanidinium dimers and tetramers around sulfate templates
    • 1:CAS:528:DyaK28XjsVKqtg%3D%3D 10.1021/ja953243d
    • Sanchez-Quesada J, Seel C, Prados P, de Mendoza J, Dalcol I, Giralt E (1996) Anion helicates: double strand helical self-assembly of chiral bicyclic guanidinium dimers and tetramers around sulfate templates. J Am Chem Soc 118(1):277-278
    • (1996) J Am Chem Soc , vol.118 , Issue.1 , pp. 277-278
    • Sanchez-Quesada, J.1    Seel, C.2    Prados, P.3    De Mendoza, J.4    Dalcol, I.5    Giralt, E.6
  • 73
    • 77951902057 scopus 로고    scopus 로고
    • Arginine-rich cell-penetrating peptides
    • Schmidt N, Mishra A, Lai G, Wong G (2009) Arginine-rich cell-penetrating peptides. FEBS Letters 584(9):1806-1813
    • (2009) FEBS Letters , vol.584 , Issue.9 , pp. 1806-1813
    • Schmidt, N.1    Mishra, A.2    Lai, G.3    Wong, G.4
  • 74
    • 84862646898 scopus 로고    scopus 로고
    • Arginine in α-defensins: Differential effects on bactericidal activity correspond to geometry of membrane curvature generation and peptide-lipid phase behavior
    • 22566697 1:CAS:528:DC%2BC38XptVWrt7g%3D 10.1074/jbc.M112.358721
    • Schmidt NW, Tai KP, Kamdar K, Mishra A, Lai GH, Zhao K, Ouellette AJ, Wong GC (2012) Arginine in α-defensins: differential effects on bactericidal activity correspond to geometry of membrane curvature generation and peptide-lipid phase behavior. J Biol Chem 287(26):21866-21872
    • (2012) J Biol Chem , vol.287 , Issue.26 , pp. 21866-21872
    • Schmidt, N.W.1    Tai, K.P.2    Kamdar, K.3    Mishra, A.4    Lai, G.H.5    Zhao, K.6    Ouellette, A.J.7    Wong, G.C.8
  • 75
    • 13344250452 scopus 로고    scopus 로고
    • Noncovalent binding between guanidinium and anionic groups: Focus on biological- and synthetic-based arginine/guanidinium interactions with phosph[on]ate and sulf[on]ate residues
    • 15720152 1:CAS:528:DC%2BD2cXhtVKktbjL 10.1021/cr040603j
    • Schug KA, Lindner W (2005) Noncovalent binding between guanidinium and anionic groups: focus on biological- and synthetic-based arginine/guanidinium interactions with phosph[on]ate and sulf[on]ate residues. Chem Rev 105:67-114
    • (2005) Chem Rev , vol.105 , pp. 67-114
    • Schug, K.A.1    Lindner, W.2
  • 76
    • 0033520487 scopus 로고    scopus 로고
    • In vivo protein transduction: Delivery of a biologically active protein into the mouse
    • 10477521 1:CAS:528:DyaK1MXlslOru78%3D 10.1126/science.285.5433.1569
    • Schwarze SR, Ho A, Vocero-Akbani A, Dowdy SF (1999) In vivo protein transduction: delivery of a biologically active protein into the mouse. Science 285(5433):1569-1572
    • (1999) Science , vol.285 , Issue.5433 , pp. 1569-1572
    • Schwarze, S.R.1    Ho, A.2    Vocero-Akbani, A.3    Dowdy, S.F.4
  • 77
    • 0034824597 scopus 로고    scopus 로고
    • From "carpet" mechanism to de novo designed diastereomeric cell-selective antimicrobial peptides
    • 11587791 1:CAS:528:DC%2BD3MXnt1SgsLg%3D 10.1016/S0196-9781(01)00498-3
    • Shai Y, Oren Z (2001) From "carpet" mechanism to de novo designed diastereomeric cell-selective antimicrobial peptides. Peptides 22(10):1629-1641
    • (2001) Peptides , vol.22 , Issue.10 , pp. 1629-1641
    • Shai, Y.1    Oren, Z.2
  • 78
    • 67649289353 scopus 로고    scopus 로고
    • The lipopolysaccharide transport system of Gram-negative bacteria
    • 19416651 1:CAS:528:DC%2BD1MXnt1GnsL4%3D 10.1016/j.bbalip.2009.01.011
    • Sperandeo P, Deho G, Polissi A (2009) The lipopolysaccharide transport system of Gram-negative bacteria. Biochim Biophys Acta 1791:594-602
    • (2009) Biochim Biophys Acta , vol.1791 , pp. 594-602
    • Sperandeo, P.1    Deho, G.2    Polissi, A.3
  • 79
    • 0019386682 scopus 로고
    • Sequence and specificity of two antimicrobial proteins involved in insect immunity
    • 7019715 1:CAS:528:DyaL38XkslyjtA%3D%3D 10.1038/292246a0
    • Steiner H, Hultmark D, Engstrom Å, Bennich H, Boman HG (1981) Sequence and specificity of two antimicrobial proteins involved in insect immunity. Nature 292:246-248
    • (1981) Nature , vol.292 , pp. 246-248
    • Steiner, H.1    Hultmark, D.2    Engstrom, Å.3    Bennich, H.4    Boman, H.G.5
  • 80
    • 80052553690 scopus 로고    scopus 로고
    • Conformational disorder of membrane peptides investigated from solid-state NMR line widths and line shapes
    • 21806038 1:CAS:528:DC%2BC3MXhtVGnurvL 10.1021/jp205002n
    • Su Y, Hong M (2011) Conformational disorder of membrane peptides investigated from solid-state NMR line widths and line shapes. J Phys Chem B 115(36):10758-10767
    • (2011) J Phys Chem B , vol.115 , Issue.36 , pp. 10758-10767
    • Su, Y.1    Hong, M.2
  • 81
    • 48749122491 scopus 로고    scopus 로고
    • Reversible sheet-turn conformational change of a cell-penetrating peptide in lipid bilayers studied by solid-state NMR
    • 18656895 1:CAS:528:DC%2BD1cXps1Gqu7o%3D 10.1016/j.jmb.2008.06.007
    • Su Y, Mani R, Doherty T, Waring AJ, Hong M (2008a) Reversible sheet-turn conformational change of a cell-penetrating peptide in lipid bilayers studied by solid-state NMR. J Mol Biol 381(5):1133-1144
    • (2008) J Mol Biol , vol.381 , Issue.5 , pp. 1133-1144
    • Su, Y.1    Mani, R.2    Doherty, T.3    Waring, A.J.4    Hong, M.5
  • 82
    • 46949096206 scopus 로고    scopus 로고
    • Asymmetric insertion of membrane proteins in lipid bilayers by solid-state NMR paramagnetic relaxation enhancement: A cell-penetrating peptide example
    • 18597439 1:CAS:528:DC%2BD1cXnt1ClsLs%3D 10.1021/ja802383t
    • Su Y, Mani R, Hong M (2008b) Asymmetric insertion of membrane proteins in lipid bilayers by solid-state NMR paramagnetic relaxation enhancement: a cell-penetrating peptide example. J Am Chem Soc 130(27):8856-8864
    • (2008) J Am Chem Soc , vol.130 , Issue.27 , pp. 8856-8864
    • Su, Y.1    Mani, R.2    Hong, M.3
  • 83
    • 66349138469 scopus 로고    scopus 로고
    • Roles of arginine and lysine residues in the translocation of a cell-penetrating peptide from 13C, 31P, and 19F solid-state NMR
    • 19364134 1:CAS:528:DC%2BD1MXlsFKrs7k%3D 10.1021/bi900080d
    • Su Y, Doherty T, Waring AJ, Ruchala P, Hong M (2009) Roles of arginine and lysine residues in the translocation of a cell-penetrating peptide from 13C, 31P, and 19F solid-state NMR. Biochemistry 48(21):4587-4595
    • (2009) Biochemistry , vol.48 , Issue.21 , pp. 4587-4595
    • Su, Y.1    Doherty, T.2    Waring, A.J.3    Ruchala, P.4    Hong, M.5
  • 84
    • 77954266293 scopus 로고    scopus 로고
    • Orientation, dynamics, and lipid interaction of an antimicrobial arylamide investigated by 19F and 31P solid-state NMR spectroscopy
    • 20536141 1:CAS:528:DC%2BC3cXntF2isbo%3D 10.1021/ja103658h
    • Su Y, DeGrado WF, Hong M (2010a) Orientation, dynamics, and lipid interaction of an antimicrobial arylamide investigated by 19F and 31P solid-state NMR spectroscopy. J Am Chem Soc 132(26):9197-9205
    • (2010) J Am Chem Soc , vol.132 , Issue.26 , pp. 9197-9205
    • Su, Y.1    Degrado, W.F.2    Hong, M.3
  • 85
    • 77954831684 scopus 로고    scopus 로고
    • Membrane-bound dynamic structure of an Arginine-rich cell-penetrating peptide, the protein transduction domain of HIV TAT, from solid-state NMR
    • 20550193 1:CAS:528:DC%2BC3cXotVSkt74%3D 10.1021/bi100642n
    • Su Y, Waring AJ, Ruchala P, Hong M (2010b) Membrane-bound dynamic structure of an Arginine-rich cell-penetrating peptide, the protein transduction domain of HIV TAT, from solid-state NMR. Biochemistry 49(29):6009-6020
    • (2010) Biochemistry , vol.49 , Issue.29 , pp. 6009-6020
    • Su, Y.1    Waring, A.J.2    Ruchala, P.3    Hong, M.4
  • 86
    • 79952980526 scopus 로고    scopus 로고
    • Structures of β-hairpin antimicrobial protegrin peptides in lipopolysaccharide membranes: Mechanism of gram selectivity obtained from solid-state nuclear magnetic resonance
    • 21302955 1:CAS:528:DC%2BC3MXit1GisLg%3D 10.1021/bi101975v
    • Su Y, Waring AJ, Ruchala P, Hong M (2011) Structures of β-hairpin antimicrobial protegrin peptides in lipopolysaccharide membranes: mechanism of gram selectivity obtained from solid-state nuclear magnetic resonance. Biochemistry 50(12):2072-2083
    • (2011) Biochemistry , vol.50 , Issue.12 , pp. 2072-2083
    • Su, Y.1    Waring, A.J.2    Ruchala, P.3    Hong, M.4
  • 87
    • 81855190866 scopus 로고    scopus 로고
    • Arginine residues are more effective than lysine residues in eliciting the cellular uptake of onconase
    • 21980976 1:CAS:528:DC%2BC3MXht1OrsbfP 10.1021/bi200979k
    • Sundlass NK, Raines RT (2011) Arginine residues are more effective than lysine residues in eliciting the cellular uptake of onconase. Biochemistry 50(47):10293-10299
    • (2011) Biochemistry , vol.50 , Issue.47 , pp. 10293-10299
    • Sundlass, N.K.1    Raines, R.T.2
  • 88
    • 33751545243 scopus 로고    scopus 로고
    • Crystal structures of human alpha-defensins HNP4, HD5, and HD6
    • 17088326 1:CAS:528:DC%2BD28XhtlSmtbzP 10.1110/ps.062336606
    • Szyk A, Wu Z, Tucker K, Yang D, Lu W, Lubkowski J (2006) Crystal structures of human alpha-defensins HNP4, HD5, and HD6. Protein Sci 15:2749-2760
    • (2006) Protein Sci , vol.15 , pp. 2749-2760
    • Szyk, A.1    Wu, Z.2    Tucker, K.3    Yang, D.4    Lu, W.5    Lubkowski, J.6
  • 89
    • 82155176225 scopus 로고    scopus 로고
    • Comparative study on the interaction of cell-penetrating polycationic polymers with lipid membranes
    • 22108318 10.1016/j.chemphyslip.2011.11.002 1:CAS:528: DC%2BC38Xht1Glug%3D%3D
    • Takechi Y, Tanaka H, Kitayama H, Yoshii H, Tanaka M, Saito H (2011) Comparative study on the interaction of cell-penetrating polycationic polymers with lipid membranes. Chem Phys Lipids 165(1):51-58
    • (2011) Chem Phys Lipids , vol.165 , Issue.1 , pp. 51-58
    • Takechi, Y.1    Tanaka, H.2    Kitayama, H.3    Yoshii, H.4    Tanaka, M.5    Saito, H.6
  • 90
    • 62949097134 scopus 로고    scopus 로고
    • Structure and mechanism of β-hairpin antimcrobial pepetides in lipid bilayers from solid-state NMR spectroscopy
    • 19396367 1:CAS:528:DC%2BD1MXjt1Kms7o%3D 10.1039/b820398a
    • Tang M, Hong M (2009) Structure and mechanism of β-hairpin antimcrobial pepetides in lipid bilayers from solid-state NMR spectroscopy. Mol BioSyst 5:317-322
    • (2009) Mol BioSyst , vol.5 , pp. 317-322
    • Tang, M.1    Hong, M.2
  • 91
    • 35048820105 scopus 로고    scopus 로고
    • Phosphate-mediated arginine insertion into lipid membranes and pore formation by a cationic membrane peptide from solid-state NMR
    • 17705480 1:CAS:528:DC%2BD2sXpt1WhsLw%3D 10.1021/ja072511s
    • Tang M, Waring AJ, Hong M (2007) Phosphate-mediated arginine insertion into lipid membranes and pore formation by a cationic membrane peptide from solid-state NMR. J Am Chem Soc 129(37):11438-11446
    • (2007) J Am Chem Soc , vol.129 , Issue.37 , pp. 11438-11446
    • Tang, M.1    Waring, A.J.2    Hong, M.3
  • 92
    • 49249088676 scopus 로고    scopus 로고
    • Arginine dynamics in a membrane-bound cationic beta-hairpin peptide from solid-state NMR
    • 18442147 1:CAS:528:DC%2BD1cXotVehsb0%3D 10.1002/cbic.200800005
    • Tang M, Waring AJ, Hong M (2008a) Arginine dynamics in a membrane-bound cationic beta-hairpin peptide from solid-state NMR. ChemBioChem 9(9):1487-1492
    • (2008) ChemBioChem , vol.9 , Issue.9 , pp. 1487-1492
    • Tang, M.1    Waring, A.J.2    Hong, M.3
  • 93
    • 45549085024 scopus 로고    scopus 로고
    • Effects of guanidinium-phosphate hydrogen bonding on the membrane-bound structure and activity of an arginine-rich membrane peptide from solid-state NMR spectroscopy
    • 18338418 1:CAS:528:DC%2BD1cXlvVCrsrk%3D 10.1002/anie.200705993
    • Tang M, Waring AJ, Lehrer RI, Hong M (2008b) Effects of guanidinium-phosphate hydrogen bonding on the membrane-bound structure and activity of an arginine-rich membrane peptide from solid-state NMR spectroscopy. Angew Chem Int Ed Engl 47(17):3202-3205
    • (2008) Angew Chem Int Ed Engl , vol.47 , Issue.17 , pp. 3202-3205
    • Tang, M.1    Waring, A.J.2    Lehrer, R.I.3    Hong, M.4
  • 94
    • 33646260897 scopus 로고    scopus 로고
    • Effect of membrane mimicking environment on the conformation of a pore-forming (xSxG)6 peptide
    • 16463358 1:CAS:528:DC%2BD28Xkt1Gkt7k%3D 10.1002/bip.20470
    • Thundimadathil J, Roeske RW, Guo L (2006) Effect of membrane mimicking environment on the conformation of a pore-forming (xSxG)6 peptide. Biopolymers 84:317-328
    • (2006) Biopolymers , vol.84 , pp. 317-328
    • Thundimadathil, J.1    Roeske, R.W.2    Guo, L.3
  • 95
    • 0035902477 scopus 로고    scopus 로고
    • TAT peptide on the surface of liposomes affords their efficient intracellular delivery even at low temperature and in the presence of metabolic inhibitors
    • 11438707 1:CAS:528:DC%2BD3MXls1Witbg%3D 10.1073/pnas.151247498
    • Torchilin VP, Rammohan R, Weissig V, Levchenko TS (2001) TAT peptide on the surface of liposomes affords their efficient intracellular delivery even at low temperature and in the presence of metabolic inhibitors. Proc Natl Acad Sci USA 98:8786-8791
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 8786-8791
    • Torchilin, V.P.1    Rammohan, R.2    Weissig, V.3    Levchenko, T.S.4
  • 96
    • 79953765150 scopus 로고    scopus 로고
    • Solid-state NMR studies of amyloid fibril structure
    • 1:CAS:528:DC%2BC3MXmsVWmtrc%3D 10.1146/annurev-physchem-032210-103539
    • Tycko R (2011) Solid-state NMR studies of amyloid fibril structure. Annu Rev Biophys Chem 62:279-299
    • (2011) Annu Rev Biophys Chem , vol.62 , pp. 279-299
    • Tycko, R.1
  • 97
    • 42449129998 scopus 로고    scopus 로고
    • Membrane adsorption, folding, insertion and translocation of synthetic trans-membrane peptides
    • 1:CAS:528:DC%2BD1cXkvFGgs7s%3D 10.1080/09687680802020313
    • Ulmschneider MB, Ulmschneider JP (2008) Membrane adsorption, folding, insertion and translocation of synthetic trans-membrane peptides. J Membr Biol 25(3):245-257
    • (2008) J Membr Biol , vol.25 , Issue.3 , pp. 245-257
    • Ulmschneider, M.B.1    Ulmschneider, J.P.2
  • 98
    • 33845343261 scopus 로고    scopus 로고
    • Membrane-protein topology
    • 10.1038/nrm2063 1:CAS:528:DC%2BD28Xht1KisrrK
    • von Heijne G (2006) Membrane-protein topology. Nat Rev Mol Cell Biol 7:909-918
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 909-918
    • Von Heijne, G.1
  • 99
    • 50549097744 scopus 로고    scopus 로고
    • Assessing atomistic and coarse-grained force fields for protein-lipid interactions: The formidable challenge of an ionizable side chain in a membrane
    • 18636764 1:CAS:528:DC%2BD1cXos1ahsr4%3D 10.1021/jp711492h
    • Vorobyov I, Li L, Allen TW (2008) Assessing atomistic and coarse-grained force fields for protein-lipid interactions: the formidable challenge of an ionizable side chain in a membrane. J Phys Chem B 112(32):9588-9602
    • (2008) J Phys Chem B , vol.112 , Issue.32 , pp. 9588-9602
    • Vorobyov, I.1    Li, L.2    Allen, T.W.3
  • 101
    • 0034700141 scopus 로고    scopus 로고
    • The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: Peptoid molecular transporters
    • 11087855 1:CAS:528:DC%2BD3cXosVKqt7o%3D 10.1073/pnas.97.24.13003
    • Wender PA, Mitchell DJ, Pattabiraman K, Pelkey ET, Steinman L, Rothbard JB (2000) The design, synthesis, and evaluation of molecules that enable or enhance cellular uptake: peptoid molecular transporters. Proc Natl Acad Sci USA 97(24):13003-13008
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.24 , pp. 13003-13008
    • Wender, P.A.1    Mitchell, D.J.2    Pattabiraman, K.3    Pelkey, E.T.4    Steinman, L.5    Rothbard, J.B.6
  • 102
    • 39149103400 scopus 로고    scopus 로고
    • The design of guanidinium-rich transporters and their internalization mechanisms
    • 18164781 1:CAS:528:DC%2BD1cXitVGnsrs%3D 10.1016/j.addr.2007.10.016
    • Wender PA, Galliher WC, Goun EA, Jones LR, Pillow TH (2008) The design of guanidinium-rich transporters and their internalization mechanisms. Adv Drug Deliv Rev 60(4-5):452
    • (2008) Adv Drug Deliv Rev , vol.60 , Issue.4-5 , pp. 452
    • Wender, P.A.1    Galliher, W.C.2    Goun, E.A.3    Jones, L.R.4    Pillow, T.H.5
  • 103
    • 0032987478 scopus 로고    scopus 로고
    • Membrane protein folding and stability: Physical principles
    • 10410805 1:CAS:528:DyaK1MXkt1erurs%3D 10.1146/annurev.biophys.28.1.319
    • White SH, Wimley WC (1999) Membrane protein folding and stability: physical principles. Annu Rev Biophys Biomol Struct 28:319-365
    • (1999) Annu Rev Biophys Biomol Struct , vol.28 , pp. 319-365
    • White, S.H.1    Wimley, W.C.2
  • 104
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • 8836100 1:CAS:528:DyaK28XmtFCrsLg%3D 10.1038/nsb1096-842
    • Wimley WC, White SH (1996) Experimentally determined hydrophobicity scale for proteins at membrane interfaces. Nat Struct Biol 3:842-848
    • (1996) Nat Struct Biol , vol.3 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 105
    • 0037031254 scopus 로고    scopus 로고
    • Solid-state NMR investigations of peptide-lipid interaction and orientation of a beta-sheet antimicrobial peptide, protegrin
    • 12146951 1:CAS:528:DC%2BD38Xltlaisr8%3D 10.1021/bi0257991
    • Yamaguchi S, Hong T, Waring A, Lehrer RI, Hong M (2002) Solid-state NMR investigations of peptide-lipid interaction and orientation of a beta-sheet antimicrobial peptide, protegrin. Biochemistry 41(31):9852-9862
    • (2002) Biochemistry , vol.41 , Issue.31 , pp. 9852-9862
    • Yamaguchi, S.1    Hong, T.2    Waring, A.3    Lehrer, R.I.4    Hong, M.5
  • 106
    • 57249091852 scopus 로고    scopus 로고
    • Medium- and long-distance 1H-13C heteronuclear correlation NMR in solids
    • 1:CAS:528:DC%2BD3MXit1ahs7g%3D 10.1006/jmre.2001.2285
    • Yao XL, Schmidt-Rohr K, Hong M (2001) Medium- and long-distance 1H-13C heteronuclear correlation NMR in solids. J Magn Reson 149(1):139-143
    • (2001) J Magn Reson , vol.149 , Issue.1 , pp. 139-143
    • Yao, X.L.1    Schmidt-Rohr, K.2    Hong, M.3
  • 107
    • 76149146426 scopus 로고    scopus 로고
    • Determination of penetratin secondary structure in live cells with Raman microscopy
    • 20041639 1:CAS:528:DC%2BD1MXhs1alurfK 10.1021/ja9043196
    • Ye J, Fox SA, Cudic M, Rezler EM, Lauer JL, Fields GB, Terentis AC (2010) Determination of penetratin secondary structure in live cells with Raman microscopy. J Am Chem Soc 132(3):980
    • (2010) J Am Chem Soc , vol.132 , Issue.3 , pp. 980
    • Ye, J.1    Fox, S.A.2    Cudic, M.3    Rezler, E.M.4    Lauer, J.L.5    Fields, G.B.6    Terentis, A.C.7
  • 108
    • 0037371597 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide action and resistance
    • 12615953 1:CAS:528:DC%2BD3sXisVKgsLg%3D 10.1124/pr.55.1.2
    • Yeaman MR, Yount NY (2003) Mechanisms of antimicrobial peptide action and resistance. Pharmacol Rev 55(1):27-55
    • (2003) Pharmacol Rev , vol.55 , Issue.1 , pp. 27-55
    • Yeaman, M.R.1    Yount, N.Y.2
  • 109
    • 43149121350 scopus 로고    scopus 로고
    • Does arginine remain protonated in the lipid membrane? Insights from microscopic pKa calculations
    • 18199662 1:CAS:528:DC%2BD1cXkt1ChtL8%3D 10.1529/biophysj.107.122945
    • Yoo J, Cui Q (2008) Does arginine remain protonated in the lipid membrane? Insights from microscopic pKa calculations. Biophys J 94(8):L61
    • (2008) Biophys J , vol.94 , Issue.8 , pp. 61
    • Yoo, J.1    Cui, Q.2
  • 110
    • 2042513493 scopus 로고
    • Magainins, a class of antimicrobial peptides from Xenopus skin: Isolation, characterization of two active forms, and partial cDNA sequence of a precursor
    • 10.1073/pnas.84.15.5449
    • Zasloff M (1987) Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor. Proc Natl Acad Sci USA 54:5449-5453
    • (1987) Proc Natl Acad Sci USA , vol.54 , pp. 5449-5453
    • Zasloff, M.1
  • 111
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M (2002) Antimicrobial peptides of multicellular organisms. Nature 415:389-395
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 112
    • 0006938812 scopus 로고    scopus 로고
    • +-l, 3-Benzimidazol-2-ylio)pyridine N-oxide dihydrogenphosphate monohydrate
    • +-l, 3-Benzimidazol-2-ylio)pyridine N-oxide dihydrogenphosphate monohydrate. Acta Crystallogr C 55:1929-1930
    • (1999) Acta Crystallogr C , vol.55 , pp. 1929-1930
    • Zhang, B.1    Liu, Y.2    Gou, S.3    Duan, C.4    You, X.5
  • 113
    • 23044477438 scopus 로고    scopus 로고
    • Mechanism of penetration of Antp(43-58) into membrane bilayers
    • 16042388 1:CAS:528:DC%2BD2MXlvVehurk%3D 10.1021/bi050341v
    • Zhang W, Smith SO (2005) Mechanism of penetration of Antp(43-58) into membrane bilayers. Biochemistry 44:10110-10118
    • (2005) Biochemistry , vol.44 , pp. 10110-10118
    • Zhang, W.1    Smith, S.O.2
  • 114
    • 77349106883 scopus 로고    scopus 로고
    • Resonance assignment and three-dimensional structure determination of a human alpha-defensin, HNP-1, by solid-state NMR
    • 20097206 1:CAS:528:DC%2BC3cXivFGqsLc%3D 10.1016/j.jmb.2010.01.030
    • Zhang Y, Doherty T, Li J, Lu W, Barinka C, Lubkowski J, Hong M (2010a) Resonance assignment and three-dimensional structure determination of a human alpha-defensin, HNP-1, by solid-state NMR. J Mol Biol 397(2):408-422
    • (2010) J Mol Biol , vol.397 , Issue.2 , pp. 408-422
    • Zhang, Y.1    Doherty, T.2    Li, J.3    Lu, W.4    Barinka, C.5    Lubkowski, J.6    Hong, M.7
  • 115
    • 78149458565 scopus 로고    scopus 로고
    • The membrane-bound structure and topology of a human α-defensin indicate a dimer pore mechanism for membrane disruption
    • 20961099 1:CAS:528:DC%2BC3cXhtleiur%2FJ 10.1021/bi101512j
    • Zhang Y, Lu W, Hong M (2010b) The membrane-bound structure and topology of a human α-defensin indicate a dimer pore mechanism for membrane disruption. Biochemistry 49(45):9770-9782
    • (2010) Biochemistry , vol.49 , Issue.45 , pp. 9770-9782
    • Zhang, Y.1    Lu, W.2    Hong, M.3
  • 116
    • 0043166977 scopus 로고    scopus 로고
    • Protein transduction domains of HIV-1 and SIV TAT interact with charged lipid vesicles. Binding mechanism and thermodynamic analysis
    • 12885253 1:CAS:528:DC%2BD3sXlt1Cht78%3D 10.1021/bi0346805
    • Ziegler A, Blatter XL, Seelig A, Seelig J (2003) Protein transduction domains of HIV-1 and SIV TAT interact with charged lipid vesicles. Binding mechanism and thermodynamic analysis. Biochemistry 42(30):9185-9194
    • (2003) Biochemistry , vol.42 , Issue.30 , pp. 9185-9194
    • Ziegler, A.1    Blatter, X.L.2    Seelig, A.3    Seelig, J.4


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