메뉴 건너뛰기




Volumn 1768, Issue 1, 2007, Pages 52-58

Conformational and functional studies of gomesin analogues by CD, EPR and fluorescence spectroscopies

Author keywords

Antimicrobial peptide; Circular dichroism; Electron paramagnetic resonance; Fluorescence; Gomesin; Solid phase peptide synthesis

Indexed keywords

2,2,6,6 TETRAMETHYLPIPERIDINE 1 OXYL 4 AMINO 4 CARBOXYLIC ACID; AMPHOLYTE; CARBOXYLIC ACID DERIVATIVE; DETERGENT; GOMESIN DERIVATIVE; POLYPEPTIDE ANTIBIOTIC AGENT; SERINE; TRYPTOPHAN;

EID: 33845536219     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2006.08.016     Document Type: Article
Times cited : (31)

References (32)
  • 1
    • 0032717048 scopus 로고    scopus 로고
    • Diversity of antimicrobial peptides and their mechanisms of action
    • Epand R.M., and Vogel H.J. Diversity of antimicrobial peptides and their mechanisms of action. Biochim. Biophys. Acta 1462 (1999) 11-28
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 11-28
    • Epand, R.M.1    Vogel, H.J.2
  • 2
    • 0037371597 scopus 로고    scopus 로고
    • Mechanisms of antimicrobial peptide action and resistance
    • Yeaman M.R., and Yount N.Y. Mechanisms of antimicrobial peptide action and resistance. Pharmacol. Rev. 55 (2003) 27-55
    • (2003) Pharmacol. Rev. , vol.55 , pp. 27-55
    • Yeaman, M.R.1    Yount, N.Y.2
  • 3
    • 0019386682 scopus 로고
    • Sequence and specificity of two antibacterial proteins involved in insect immunity
    • Steiner H., Hultmark D., Engstrom A., Bennich H., and Boman H.G. Sequence and specificity of two antibacterial proteins involved in insect immunity. Nature 292 (1981) 246-248
    • (1981) Nature , vol.292 , pp. 246-248
    • Steiner, H.1    Hultmark, D.2    Engstrom, A.3    Bennich, H.4    Boman, H.G.5
  • 4
    • 0032411402 scopus 로고    scopus 로고
    • Cysteine-rich antimicrobial peptides in invertebrates
    • Dimarcq J.L., Bulet P., Hetru C., and Hoffmann J. Cysteine-rich antimicrobial peptides in invertebrates. Biopolymers 47 (1998) 465-477
    • (1998) Biopolymers , vol.47 , pp. 465-477
    • Dimarcq, J.L.1    Bulet, P.2    Hetru, C.3    Hoffmann, J.4
  • 5
  • 6
    • 33645739232 scopus 로고    scopus 로고
    • Structure-activity relationship studies of gomesin: importance of the disulfide bridges for conformation, bioactivities and serum stability
    • Fázio M.A., Daffre S., Miranda M.T.M., and Miranda A. Structure-activity relationship studies of gomesin: importance of the disulfide bridges for conformation, bioactivities and serum stability. Biopolymers 84 (2006) 205-218
    • (2006) Biopolymers , vol.84 , pp. 205-218
    • Fázio, M.A.1    Daffre, S.2    Miranda, M.T.M.3    Miranda, A.4
  • 7
    • 32544456244 scopus 로고    scopus 로고
    • Antimicrobial peptides: new candidates in the fight against bacterial infections
    • Toke O. Antimicrobial peptides: new candidates in the fight against bacterial infections. Biopolymers 80 (2005) 717-735
    • (2005) Biopolymers , vol.80 , pp. 717-735
    • Toke, O.1
  • 8
    • 0032693639 scopus 로고    scopus 로고
    • Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes
    • Matsuzaki K. Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes. BBA-Biomembranes 1462 (1999) 1-10
    • (1999) BBA-Biomembranes , vol.1462 , pp. 1-10
    • Matsuzaki, K.1
  • 9
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides
    • Shai Y. Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides. Biochim. Biophys. Acta 1462 (1999) 55-70
    • (1999) Biochim. Biophys. Acta , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 10
    • 0034721871 scopus 로고    scopus 로고
    • Isolation and characterization of gomesin, an 18-residue cysteine-rich defense peptide from the spider Acanthoscurria gomesiana hemocytes with sequence similarities to horseshoe crab antimicrobial peptides of the tachyplesin family
    • Silva Jr. P.I., Daffre S., and Bulet P. Isolation and characterization of gomesin, an 18-residue cysteine-rich defense peptide from the spider Acanthoscurria gomesiana hemocytes with sequence similarities to horseshoe crab antimicrobial peptides of the tachyplesin family. J. Biol. Chem. 275 (2000) 33464-33470
    • (2000) J. Biol. Chem. , vol.275 , pp. 33464-33470
    • Silva Jr., P.I.1    Daffre, S.2    Bulet, P.3
  • 11
    • 0036178451 scopus 로고    scopus 로고
    • The solution structure of gomesin, an antimicrobial cysteine-rich peptide from the spider
    • Mandard N., Bulet P., Caille A., Daffre S., and Vovelle F. The solution structure of gomesin, an antimicrobial cysteine-rich peptide from the spider. Eur. J. Biochem. 269 (2002) 1190-1198
    • (2002) Eur. J. Biochem. , vol.269 , pp. 1190-1198
    • Mandard, N.1    Bulet, P.2    Caille, A.3    Daffre, S.4    Vovelle, F.5
  • 12
    • 0023700978 scopus 로고
    • Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus tridentatus). Isolation and chemical structure
    • Nakamura T., Furunaka H., Miyata T., Tokunaga F., Muta T., Iwanaga S., Niwa M., Takao T., and Shimonishi Y. Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus tridentatus). Isolation and chemical structure. J. Biol. Chem. 263 (1988) 16709-16713
    • (1988) J. Biol. Chem. , vol.263 , pp. 16709-16713
    • Nakamura, T.1    Furunaka, H.2    Miyata, T.3    Tokunaga, F.4    Muta, T.5    Iwanaga, S.6    Niwa, M.7    Takao, T.8    Shimonishi, Y.9
  • 13
    • 0024741960 scopus 로고
    • Antimicrobial peptides, isolated from horseshoe crab hemocytes, tachyplesin II, and polyphemusins I and II: chemical structures and biological activity
    • (Tokyo)
    • Miyata T., Tokunaga F., Yoneya T., Yoshikawa K., Iwanaga S., Niwa M., Takao T., and Shimonishi Y. Antimicrobial peptides, isolated from horseshoe crab hemocytes, tachyplesin II, and polyphemusins I and II: chemical structures and biological activity. J. Biochem. 106 (1989) 663-668 (Tokyo)
    • (1989) J. Biochem. , vol.106 , pp. 663-668
    • Miyata, T.1    Tokunaga, F.2    Yoneya, T.3    Yoshikawa, K.4    Iwanaga, S.5    Niwa, M.6    Takao, T.7    Shimonishi, Y.8
  • 14
    • 0030449497 scopus 로고    scopus 로고
    • Endogenous vertebrate antibiotics. Defensins, protegrins, and other cysteine-rich antimicrobial peptides
    • Lehrer R., and Ganz T. Endogenous vertebrate antibiotics. Defensins, protegrins, and other cysteine-rich antimicrobial peptides. Ann. N.Y. Acad. Sci. 797 (1996) 228-239
    • (1996) Ann. N.Y. Acad. Sci. , vol.797 , pp. 228-239
    • Lehrer, R.1    Ganz, T.2
  • 16
    • 12044255745 scopus 로고
    • A novel spin labeled amino acid derivative for use in peptide synthesis: (9-fluorenylmethyloxy-carbonyl)-2,2,6,6-tetramethyl piperidine-N-oxyl-4-amino-4-carboxylic acid
    • Marchetto R., Schreier S., and Nakaie C.R. A novel spin labeled amino acid derivative for use in peptide synthesis: (9-fluorenylmethyloxy-carbonyl)-2,2,6,6-tetramethyl piperidine-N-oxyl-4-amino-4-carboxylic acid. J. Am. Chem. Soc. 115 (1993) 11042-11043
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 11042-11043
    • Marchetto, R.1    Schreier, S.2    Nakaie, C.R.3
  • 20
  • 21
    • 0035821306 scopus 로고    scopus 로고
    • Effect of temperature on peptide chain aggregation: an EPR study of model peptidyl-resins
    • Ribeiro S.C.F., Schreier S., Nakaie C.R., and Cilli E.M. Effect of temperature on peptide chain aggregation: an EPR study of model peptidyl-resins. Tetrahedron Lett. 42 (2001) 3243-3246
    • (2001) Tetrahedron Lett. , vol.42 , pp. 3243-3246
    • Ribeiro, S.C.F.1    Schreier, S.2    Nakaie, C.R.3    Cilli, E.M.4
  • 22
    • 0037274881 scopus 로고    scopus 로고
    • Interaction of peptides with binary phospholipid membranes: application of fluorescence methodologies
    • Loura L.M.S., Almeida R.F.M., Coutinho A., and Prieto M. Interaction of peptides with binary phospholipid membranes: application of fluorescence methodologies. Chem. Phys. Lipids 122 (2003) 77-96
    • (2003) Chem. Phys. Lipids , vol.122 , pp. 77-96
    • Loura, L.M.S.1    Almeida, R.F.M.2    Coutinho, A.3    Prieto, M.4
  • 25
    • 0031871596 scopus 로고    scopus 로고
    • TOAC, a nitroxide spin-labeled, achiral C-alpha-tetrasubstituted alpha-amino acid, is an excellent tool in material science and biochemistry
    • Toniolo C., Crisma M., and Formaggio F. TOAC, a nitroxide spin-labeled, achiral C-alpha-tetrasubstituted alpha-amino acid, is an excellent tool in material science and biochemistry. Biopolymers 47 (1998) 153-158
    • (1998) Biopolymers , vol.47 , pp. 153-158
    • Toniolo, C.1    Crisma, M.2    Formaggio, F.3
  • 27
    • 0027528472 scopus 로고
    • Function and chemical characterization of Hymenoptaecin, an antibacterial polypeptide that is infection-inducible in the honeybee (Apis mellifera)
    • Casteels P., Ampe C., Jacobs F., and Tempst P. Function and chemical characterization of Hymenoptaecin, an antibacterial polypeptide that is infection-inducible in the honeybee (Apis mellifera). J. Biol. Chem. 268 (1993) 7044-7054
    • (1993) J. Biol. Chem. , vol.268 , pp. 7044-7054
    • Casteels, P.1    Ampe, C.2    Jacobs, F.3    Tempst, P.4
  • 28
    • 3843152597 scopus 로고    scopus 로고
    • Conformational basis for the biological activity of TOAC-labeled angiotensin II and Bradykinin: electron paramagnetic resonance, circular dichroism, and fluorescence studies
    • Schreier S., Barbosa S.R., Casallanovo F., Vieira R.F.F., Cilli E.M., Paiva A.C.M., and Nakaie C.R. Conformational basis for the biological activity of TOAC-labeled angiotensin II and Bradykinin: electron paramagnetic resonance, circular dichroism, and fluorescence studies. Biopolymers 74 (2004) 389-402
    • (2004) Biopolymers , vol.74 , pp. 389-402
    • Schreier, S.1    Barbosa, S.R.2    Casallanovo, F.3    Vieira, R.F.F.4    Cilli, E.M.5    Paiva, A.C.M.6    Nakaie, C.R.7
  • 29
    • 0014592230 scopus 로고
    • Computed circular dichroism spectra for evaluation of protein conformation
    • Greenfield N., and Fasman G. Computed circular dichroism spectra for evaluation of protein conformation. Biochemistry 8 (1969) 4116
    • (1969) Biochemistry , vol.8 , pp. 4116
    • Greenfield, N.1    Fasman, G.2
  • 31
    • 0028978422 scopus 로고
    • Trifluoroethanol-induced stabilization of the α-helical structure of β-lactoglobulin: implication for non-hierarchical protein folding
    • Shiraki J., Nishikawa K., and Goto Y. Trifluoroethanol-induced stabilization of the α-helical structure of β-lactoglobulin: implication for non-hierarchical protein folding. J. Mol. Biol. 245 (1995) 180-194
    • (1995) J. Mol. Biol. , vol.245 , pp. 180-194
    • Shiraki, J.1    Nishikawa, K.2    Goto, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.