메뉴 건너뛰기




Volumn 17, Issue 3, 2011, Pages 211-217

Synthesis, biological activity and solution structure of new analogues of the antimicrobial Gramicidin S

Author keywords

Amphipathicity; Antimicrobial peptide; Cyclic peptide synthesis; Gramicidin S; Hemolysis; Molecular dynamics; NMR; Structure activity relationship

Indexed keywords

CYCLOPEPTIDE; GRAMICIDIN S; GRAMICIDIN S10 0; GRAMICIDIN S10 1; GRAMICIDIN S10 2; GRAMICIDIN S10 3; UNCLASSIFIED DRUG;

EID: 79751515595     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.1314     Document Type: Article
Times cited : (11)

References (39)
  • 1
    • 0001131165 scopus 로고
    • Gramicidin S and its use in the treatment of infected wounds
    • Gause GF, Brazhnikova MG. Gramicidin S and its use in the treatment of infected wounds. Nature 1944; 154: 703.
    • (1944) Nature , vol.154 , pp. 703
    • Gause, G.F.1    Brazhnikova, M.G.2
  • 2
    • 0014348183 scopus 로고
    • A Conformational analysis of gramicidin S-A by nuclear magnetic resonance
    • Stern A, Gibbons WA, Craig LC. A Conformational analysis of gramicidin S-A by nuclear magnetic resonance. Proc. Natl. Acad. Sci. U. S. A. 1968; 61: 734-741.
    • (1968) Proc. Natl. Acad. Sci. U. S. A. , vol.61 , pp. 734-741
    • Stern, A.1    Gibbons, W.A.2    Craig, L.C.3
  • 3
    • 0019258451 scopus 로고
    • Intermolecular anti-parallel β sheet: comparison of predicted and observed conformations of gramicidin S
    • Rackovsky S, Scheraga HA. Intermolecular anti-parallel β sheet: comparison of predicted and observed conformations of gramicidin S. Proc. Natl. Acad. Sci. U. S. A. 1980; 77: 6965-6967.
    • (1980) Proc. Natl. Acad. Sci. U. S. A. , vol.77 , pp. 6965-6967
    • Rackovsky, S.1    Scheraga, H.A.2
  • 4
    • 0003417490 scopus 로고
    • Synthetic Aspects of Biologically Active Cyclic Peptides: Gramicidin S and Tyrocidines
    • Halsted Press: New York.
    • Izumiya N, Kato T, Aoyaga H, Waki M, Kondo M. Synthetic Aspects of Biologically Active Cyclic Peptides: Gramicidin S and Tyrocidines. Halsted Press: New York, 1979; 49-89.
    • (1979) , pp. 49-89
    • Izumiya, N.1    Kato, T.2    Aoyaga, H.3    Waki, M.4    Kondo, M.5
  • 5
    • 0029816946 scopus 로고    scopus 로고
    • Modulation of structure and antibacterial and hemolytic activity by ring size in cyclic gramicidin S analogs
    • Kondejewski LH, Farmer SW, Wishart DS, Kay CM, Hancock REW, Hodges RS. Modulation of structure and antibacterial and hemolytic activity by ring size in cyclic gramicidin S analogs. J. Biol. Chem. 1996; 271: 25261-25268.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25261-25268
    • Kondejewski, L.H.1    Farmer, S.W.2    Wishart, D.S.3    Kay, C.M.4    Hancock, R.E.W.5    Hodges, R.S.6
  • 7
    • 0037539998 scopus 로고    scopus 로고
    • Structure-activity relationships of de novo designed cyclic antimicrobial peptides based on gramicidin S
    • Lee DL, Hodges RS. Structure-activity relationships of de novo designed cyclic antimicrobial peptides based on gramicidin S. Biopolymers 2003; 71: 28-48.
    • (2003) Biopolymers , vol.71 , pp. 28-48
    • Lee, D.L.1    Hodges, R.S.2
  • 8
    • 15044360966 scopus 로고    scopus 로고
    • Studies on the synthetic methodology of head to tail cyclization of linear peptides
    • Yun-hua Y, Xing-ming G, Mian L, Yan-chun T, Gui-ling Tian. Studies on the synthetic methodology of head to tail cyclization of linear peptides. Lett. Pept. Sci. 2003; 10: 571-579.
    • (2003) Lett. Pept. Sci. , vol.10 , pp. 571-579
    • Yun-hua, Y.1    Xing-ming, G.2    Mian, L.3    Yan-chun, T.4    Gui-ling, T.5
  • 9
    • 0035991443 scopus 로고    scopus 로고
    • Synthesis of cyclopentapeptides and cycloheptapeptides by DEPBT and the influence of some factors on cyclization
    • Tang YC, Xie HB, Tian GL, Ye YH. Synthesis of cyclopentapeptides and cycloheptapeptides by DEPBT and the influence of some factors on cyclization. J. Pept. Res. 2002; 60: 95-103.
    • (2002) J. Pept. Res. , vol.60 , pp. 95-103
    • Tang, Y.C.1    Xie, H.B.2    Tian, G.L.3    Ye, Y.H.4
  • 10
    • 0342644832 scopus 로고    scopus 로고
    • A comparative study of cyclization strategies applied to the synthesis of head-to-tail cyclic analogs of a viral epitope
    • Valero ML, Giralt E, Andreu D. A comparative study of cyclization strategies applied to the synthesis of head-to-tail cyclic analogs of a viral epitope. J. Pept. Res. 1999; 53: 56-67.
    • (1999) J. Pept. Res. , vol.53 , pp. 56-67
    • Valero, M.L.1    Giralt, E.2    Andreu, D.3
  • 12
    • 0025767755 scopus 로고
    • 2-Chlorotrityl chloride resin. Studies on anchoring of Fmoc-amino acids and peptide cleavage
    • Barlos K, Chatzi O, Gatos D, Stavropoulos G. 2-Chlorotrityl chloride resin. Studies on anchoring of Fmoc-amino acids and peptide cleavage. Int. J. Pept. Protein Res. 1991; 37: 513-520.
    • (1991) Int. J. Pept. Protein Res. , vol.37 , pp. 513-520
    • Barlos, K.1    Chatzi, O.2    Gatos, D.3    Stavropoulos, G.4
  • 13
    • 0026338002 scopus 로고
    • Application of 2-chlorotrityl resin in solid phase synthesis of (Leu15)-gastrin I and unsulfated cholecystokinin octapeptide. Selective O-deprotection of tyrosine
    • Barlos K, Gatos D, Kapolos S, Poulos C, Schäfer W, Yao WQ. Application of 2-chlorotrityl resin in solid phase synthesis of (Leu15)-gastrin I and unsulfated cholecystokinin octapeptide. Selective O-deprotection of tyrosine. Int. J. Pept. Protein Res. 1991; 38(6): 555-561.
    • (1991) Int. J. Pept. Protein Res. , vol.38 , Issue.6 , pp. 555-561
    • Barlos, K.1    Gatos, D.2    Kapolos, S.3    Poulos, C.4    Schäfer, W.5    Yao, W.Q.6
  • 14
    • 0042646053 scopus 로고    scopus 로고
    • New strategy for the synthesis of large peptides as applied to the C-terminal cysteine-rich 41 amino acid fragment of the mouse agouti protein
    • Bodi J, Suli-Vargha H, Ludanyi K, Vekey K, Orosz G. New strategy for the synthesis of large peptides as applied to the C-terminal cysteine-rich 41 amino acid fragment of the mouse agouti protein. Tetrahedron Lett. 1997; 38: 3293-3296.
    • (1997) Tetrahedron Lett. , vol.38 , pp. 3293-3296
    • Bodi, J.1    Suli-Vargha, H.2    Ludanyi, K.3    Vekey, K.4    Orosz, G.5
  • 15
    • 0029874669 scopus 로고    scopus 로고
    • Synthesis of the very acid-sensitive Fmoc-Cys(Mmt)-OH and its application in solid-phase peptide synthesis
    • Barlos K, Gatos D, Hatzi O, Koch N, Koutsogianni S. Synthesis of the very acid-sensitive Fmoc-Cys(Mmt)-OH and its application in solid-phase peptide synthesis. Int. J. Pept. Protein Res. 1996; 47(3): 148-153.
    • (1996) Int. J. Pept. Protein Res. , vol.47 , Issue.3 , pp. 148-153
    • Barlos, K.1    Gatos, D.2    Hatzi, O.3    Koch, N.4    Koutsogianni, S.5
  • 16
    • 0003714939 scopus 로고    scopus 로고
    • FMOC Solid Phase Peptide Synthesis. A Practical Approach
    • Oxford University Press: Oxford.
    • Chan WC, White PD. FMOC Solid Phase Peptide Synthesis. A Practical Approach. Oxford University Press: Oxford, 2000.
    • (2000)
    • Chan, W.C.1    White, P.D.2
  • 17
    • 3142580423 scopus 로고    scopus 로고
    • Fast and efficient purification of synthetic peptides by solid-phase extraction
    • Kamysz W, Okrój M, œempicka E, Ossowski T, œukasiak J. Fast and efficient purification of synthetic peptides by solid-phase extraction. Acta Chromatogr. 2004; 14: 180-186.
    • (2004) Acta Chromatogr. , vol.14 , pp. 180-186
    • Kamysz, W.1    Okrój, M.2    œempicka, E.3    Ossowski, T.4    œukasiak, J.5
  • 18
    • 79751482353 scopus 로고    scopus 로고
    • Varian. Nuclear Magnetic Resonance Instruments, VnmrTM Software. Palo Alto, CA, Revision 5.3B 1/97.
    • Varian. Nuclear Magnetic Resonance Instruments, VnmrTM Software. Palo Alto, CA, 2002; Revision 5.3B 1/97.
    • (2002)
  • 19
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
    • Bartles C, Xia T, Billeter M, Güntert P, Wütrich K. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. J. Biomol. NMR 1995; 6: 1-10.
    • (1995) J. Biomol. NMR , vol.6 , pp. 1-10
    • Bartles, C.1    Xia, T.2    Billeter, M.3    Güntert, P.4    Wütrich, K.5
  • 20
    • 0003919736 scopus 로고
    • NMR of Proteins and Nucleic Acids
    • Wiley Interscience: New York
    • Wüthrich K. NMR of Proteins and Nucleic Acids. Wiley Interscience: New York, 1986.
    • (1986)
    • Wüthrich, K.1
  • 21
    • 0026089657 scopus 로고
    • Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA
    • Güntert P, Braun W, Wüthrich K. Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA. J. Mol. Biol. 1991; 217: 517-530.
    • (1991) J. Mol. Biol. , vol.217 , pp. 517-530
    • Güntert, P.1    Braun, W.2    Wüthrich, K.3
  • 22
    • 0026259488 scopus 로고
    • Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints
    • Güntert P, Wüthrich K. Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints. J. Biomol. NMR. 1991; 1: 447-456.
    • (1991) J. Biomol. NMR. , vol.1 , pp. 447-456
    • Güntert, P.1    Wüthrich, K.2
  • 23
    • 33745356391 scopus 로고
    • Contact Electron-Spin Coupling of Nuclear Magnetic Moments
    • Karplus M. Contact Electron-Spin Coupling of Nuclear Magnetic Moments. J. Phys. Chem. 1959; 30: 11-15.
    • (1959) J. Phys. Chem. , vol.30 , pp. 11-15
    • Karplus, M.1
  • 24
    • 0347610773 scopus 로고
    • 13C nuclear magnetic resonance chemical shifts
    • 13C nuclear magnetic resonance chemical shifts. J. Am. Chem. Soc. 1991; 113: 5490-5492.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 5490-5492
    • Spera, S.1    Bax, A.2
  • 25
    • 0000437307 scopus 로고
    • Time-dependent distance restraints in molecular dynamics simulations
    • Torda AE, Scheek RM, van Gunsteren WF. Time-dependent distance restraints in molecular dynamics simulations. Chem. Phys. Lett. 1989; 157: 289-294.
    • (1989) Chem. Phys. Lett. , vol.157 , pp. 289-294
    • Torda, A.E.1    Scheek, R.M.2    van Gunsteren, W.F.3
  • 26
    • 0025778738 scopus 로고
    • Are time-averaged restraints necessary for nuclear magnetic resonance refinement? A model study for DNA
    • Pearlman DA, Kollman PA. Are time-averaged restraints necessary for nuclear magnetic resonance refinement? A model study for DNA. J. Mol. Biol. 1991; 220: 457-479.
    • (1991) J. Mol. Biol. , vol.220 , pp. 457-479
    • Pearlman, D.A.1    Kollman, P.A.2
  • 28
    • 84988053694 scopus 로고
    • An all atom forcefield for simulations of proteins and nucleic acid
    • Weiner SJ, Kollman PA, Nguyen DT, Case DA. An all atom forcefield for simulations of proteins and nucleic acid. J. Comput. Chem. 1986; 7: 230-252.
    • (1986) J. Comput. Chem. , vol.7 , pp. 230-252
    • Weiner, S.J.1    Kollman, P.A.2    Nguyen, D.T.3    Case, D.A.4
  • 29
    • 0000020246 scopus 로고    scopus 로고
    • A five-site model liquid water and the reproduction of the density anomaly by rigid, non-polarizable models
    • Mahoney MW, Jorgensen WL. A five-site model liquid water and the reproduction of the density anomaly by rigid, non-polarizable models. J. Chem. Phys. 2000; 112: 8910-8922.
    • (2000) J. Chem. Phys. , vol.112 , pp. 8910-8922
    • Mahoney, M.W.1    Jorgensen, W.L.2
  • 30
    • 33846823909 scopus 로고
    • Particle Mesh Ewald-an N. Log(N) method for Ewald sums in large systems
    • Darden T, York D, Pedersen L. Particle Mesh Ewald-an N. Log(N) method for Ewald sums in large systems. J. Chem. Phys. 1993; 98: 10089-10092.
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 31
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: a program for display and analysis of macromolecular structures
    • Koradi R, Billeter M, Wütrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 1996; 14(1): 51-55.
    • (1996) J. Mol. Graph. , vol.14 , Issue.1 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wütrich, K.3
  • 32
    • 0033593405 scopus 로고    scopus 로고
    • Cyclisation of histidine containing peptides in the solid-phase by anchoring the imidazole ring to trityl resins
    • Sabatino G, Chelli M, Mazzucco S, Ginanneschi M, Papini AM. Cyclisation of histidine containing peptides in the solid-phase by anchoring the imidazole ring to trityl resins. Tetrahedron Lett. 1999; 40: 809-812.
    • (1999) Tetrahedron Lett. , vol.40 , pp. 809-812
    • Sabatino, G.1    Chelli, M.2    Mazzucco, S.3    Ginanneschi, M.4    Papini, A.M.5
  • 34
    • 3843049165 scopus 로고    scopus 로고
    • An improved method for the solution cyclization of peptides under pseudo-high dilution conditions
    • Malesevic M, Strijowski U, Bächle D, Sewald N. An improved method for the solution cyclization of peptides under pseudo-high dilution conditions. J. Biotechnol. 2004; 112: 73-77.
    • (2004) J. Biotechnol. , vol.112 , pp. 73-77
    • Malesevic, M.1    Strijowski, U.2    Bächle, D.3    Sewald, N.4
  • 35
    • 64549117769 scopus 로고    scopus 로고
    • Effect of ring size on conformation and biological activity of cyclic cationic antimicrobial peptides
    • Jelokhani-Niaraki M, Kondejewski LH, Wheaton LC, Hodges RS. Effect of ring size on conformation and biological activity of cyclic cationic antimicrobial peptides. J. Med. Chem. 2009; 52: 2090-2097.
    • (2009) J. Med. Chem. , vol.52 , pp. 2090-2097
    • Jelokhani-Niaraki, M.1    Kondejewski, L.H.2    Wheaton, L.C.3    Hodges, R.S.4
  • 36
    • 0024278597 scopus 로고
    • Folding of immunogenic peptide fragments of proteins in water solution: I. Sequence requirements for the formation of a reverse turn
    • Dyson HJ, Rance M, Houghten RA, Lemer RA, Wright PE. Folding of immunogenic peptide fragments of proteins in water solution: I. Sequence requirements for the formation of a reverse turn. J. Mol. Biol. 1988; 201: 161-200.
    • (1988) J. Mol. Biol. , vol.201 , pp. 161-200
    • Dyson, H.J.1    Rance, M.2    Houghten, R.A.3    Lemer, R.A.4    Wright, P.E.5
  • 37
    • 0004000681 scopus 로고
    • Biomolecular NMR Spectroscopy
    • Oxford University Press: Oxford
    • Evans JNS. Biomolecular NMR Spectroscopy. Oxford University Press: Oxford, 1995.
    • (1995)
    • Evans, J.N.S.1
  • 38
    • 0026597879 scopus 로고
    • The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
    • Wishart DS, Sykes BD, Richards FM. The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry 1992; 31: 1647-1651.
    • (1992) Biochemistry , vol.31 , pp. 1647-1651
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 39
    • 79751504330 scopus 로고
    • Biostereochemia
    • Wydawnictwo Naukowe PWN: Warszawa
    • Siemion IZ. Biostereochemia. Wydawnictwo Naukowe PWN: Warszawa, 1985.
    • (1985)
    • Siemion, I.Z.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.