메뉴 건너뛰기




Volumn 14, Issue 4, 2008, Pages 436-441

The conformation of fusogenic B18 peptide in surfactant solutions

Author keywords

B18 peptide; Charged and nonionic surfactants; Circular dichroism; Conformattonal analysis; Fluorescence measurements

Indexed keywords

MEMBRANE PROTEIN; MONOMER; NONIONIC SURFACTANT; PEPTIDE B18; SURFACTANT; UNCLASSIFIED DRUG;

EID: 42149089842     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.935     Document Type: Article
Times cited : (9)

References (22)
  • 2
    • 0037926157 scopus 로고    scopus 로고
    • Peptides and membrane fusion: Towards an understanding of the molecular mechanism of protein-induced fusion
    • Pécheur EI, Sainte-Marie J, Bienvenüe A, Hoekstra D. Peptides and membrane fusion: towards an understanding of the molecular mechanism of protein-induced fusion. J. Membr. Biol. 1999; 167: 1-17.
    • (1999) J. Membr. Biol , vol.167 , pp. 1-17
    • Pécheur, E.I.1    Sainte-Marie, J.2    Bienvenüe, A.3    Hoekstra, D.4
  • 3
    • 0034444121 scopus 로고    scopus 로고
    • Viral fusion peptides: A tool set to disrupt and connect biological membranes
    • Tamm LK, Han X. Viral fusion peptides: a tool set to disrupt and connect biological membranes. Biosci. Rep. 2000; 20: 501-518.
    • (2000) Biosci. Rep , vol.20 , pp. 501-518
    • Tamm, L.K.1    Han, X.2
  • 4
    • 0027518669 scopus 로고
    • Characterization of the membrane-associating domain of the sperm adhesive protein bindin
    • Miraglia SJ, Glabe CG. Characterization of the membrane-associating domain of the sperm adhesive protein bindin. Biochem. Biophys. Acta 1993; 1145: 191-198.
    • (1993) Biochem. Biophys. Acta , vol.1145 , pp. 191-198
    • Miraglia, S.J.1    Glabe, C.G.2
  • 5
    • 0032479148 scopus 로고    scopus 로고
    • Membrane fusion is induced by a distinct peptide sequence of the sea urchin fertilization protein bindin
    • Ulrich AS, Otter M, Glabe CG, Hoekstra D. Membrane fusion is induced by a distinct peptide sequence of the sea urchin fertilization protein bindin. J. Biol. Chem. 1998; 273: 16748-16755.
    • (1998) J. Biol. Chem , vol.273 , pp. 16748-16755
    • Ulrich, A.S.1    Otter, M.2    Glabe, C.G.3    Hoekstra, D.4
  • 6
    • 0039256708 scopus 로고    scopus 로고
    • Structure analysis of a fusogenic peptide sequence from the sea urchin fertilization protein bindin
    • Glaser RW, Grüne M, Wandelt C, Ulrich AS. Structure analysis of a fusogenic peptide sequence from the sea urchin fertilization protein bindin. Biochemistry 1999; 38: 2560-2569.
    • (1999) Biochemistry , vol.38 , pp. 2560-2569
    • Glaser, R.W.1    Grüne, M.2    Wandelt, C.3    Ulrich, A.S.4
  • 7
    • 0032796075 scopus 로고    scopus 로고
    • Ultrastructural characterization of peptide-induced membrane fusion and peptide self-assembly in lipid bilayer
    • Ulrich AS, Tichelaar W, Förster G, Zschörnig O, Weinkauf S, Meyer HW. Ultrastructural characterization of peptide-induced membrane fusion and peptide self-assembly in lipid bilayer. Biophys. J. 1999; 77: 829-841.
    • (1999) Biophys. J , vol.77 , pp. 829-841
    • Ulrich, A.S.1    Tichelaar, W.2    Förster, G.3    Zschörnig, O.4    Weinkauf, S.5    Meyer, H.W.6
  • 8
    • 0034730455 scopus 로고    scopus 로고
    • The effect of Zn2+ on the secondary structure of a histidine-ricb fusogenic peptide and its interaction with lipid membranes
    • Binder H, Arnold K, Ulrich AS, Zschörnig O. The effect of Zn2+ on the secondary structure of a histidine-ricb fusogenic peptide and its interaction with lipid membranes. Biochim. Biophys. Acta 2000; 1468: 345-358.
    • (2000) Biochim. Biophys. Acta , vol.1468 , pp. 345-358
    • Binder, H.1    Arnold, K.2    Ulrich, A.S.3    Zschörnig, O.4
  • 9
    • 0842329183 scopus 로고    scopus 로고
    • Boomerang'-like insertion of a fusogenic peptide in a lipid membrane revealed by solid-state 19F NMR
    • Afonin S, Dürr UHN, Glaser RW, Ulrich AS. Boomerang'-like insertion of a fusogenic peptide in a lipid membrane revealed by solid-state 19F NMR. Magn. Reson. Chem. 2004; 42: 195-203.
    • (2004) Magn. Reson. Chem , vol.42 , pp. 195-203
    • Afonin, S.1    Dürr, U.H.N.2    Glaser, R.W.3    Ulrich, A.S.4
  • 10
    • 0037489349 scopus 로고    scopus 로고
    • Structural and dynamical changes of the bindin B18 peptide upon binding to lipid membranes. A solid-state NMR study
    • Barré P, Zschörnig O, Arnold K, Huster D. Structural and dynamical changes of the bindin B18 peptide upon binding to lipid membranes. A solid-state NMR study. Biochemistry 2003; 42: 8377-8386.
    • (2003) Biochemistry , vol.42 , pp. 8377-8386
    • Barré, P.1    Zschörnig, O.2    Arnold, K.3    Huster, D.4
  • 11
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • Sreerama N, Woody RW. Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal. Biochem. 2000; 287: 252-260.
    • (2000) Anal. Biochem , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 13
    • 0021139131 scopus 로고
    • Fluorimetric determination of critical micelle concentration avoiding interference from detergent charge
    • Chattopadhyay A, London E. Fluorimetric determination of critical micelle concentration avoiding interference from detergent charge. Anal. Biochem. 1984; 139: 408-412.
    • (1984) Anal. Biochem , vol.139 , pp. 408-412
    • Chattopadhyay, A.1    London, E.2
  • 17
    • 0034476605 scopus 로고    scopus 로고
    • Determination of micelle structure of octyl-beta-glucoside in aqueous solution by small angle neutron scattering and geometric analysis
    • He LZ, Garamus V, Niemeyer B, Helmholz H, Willumeit R Determination of micelle structure of octyl-beta-glucoside in aqueous solution by small angle neutron scattering and geometric analysis. J. Mol. Liq. 2000: 89: 239-249.
    • (2000) J. Mol. Liq , vol.89 , pp. 239-249
    • He, L.Z.1    Garamus, V.2    Niemeyer, B.3    Helmholz, H.4    Willumeit, R.5
  • 18
    • 0002104663 scopus 로고
    • The flattening of the absorption spectrum of suspensions, as compared to that of solutions
    • Duysens LNM. The flattening of the absorption spectrum of suspensions, as compared to that of solutions. Biochim. Biophys. Acta 1956; 19: 1-12.
    • (1956) Biochim. Biophys. Acta , vol.19 , pp. 1-12
    • Duysens, L.N.M.1
  • 19
    • 0011293747 scopus 로고
    • Nucleation in premicellar aggregation
    • Loran CP, von Wandruszka R. Nucleation in premicellar aggregation. Talanta 1991; 38: 497-501.
    • (1991) Talanta , vol.38 , pp. 497-501
    • Loran, C.P.1    von Wandruszka, R.2
  • 20
    • 28444449525 scopus 로고    scopus 로고
    • Interactions between charged polypeptides and nonionic surfactants
    • Sjögren H, Ericsson CA, Evenäs J, Ulvenlund S. Interactions between charged polypeptides and nonionic surfactants. Biophys. J. 2005; 89: 4219-4233.
    • (2005) Biophys. J , vol.89 , pp. 4219-4233
    • Sjögren, H.1    Ericsson, C.A.2    Evenäs, J.3    Ulvenlund, S.4
  • 21
    • 4744341349 scopus 로고
    • Polymer-micelle interactions: Physical organic aspects
    • Brackman JC, Engberts JBFN. Polymer-micelle interactions: physical organic aspects. Chem. Soc. Rev. 1993; 22: 85-92.
    • (1993) Chem. Soc. Rev , vol.22 , pp. 85-92
    • Brackman, J.C.1    Engberts, J.B.F.N.2
  • 22
    • 0024107330 scopus 로고
    • Polymer-nonionic micelle complexation. Formation of poly(propyleneoxide)-complex n-octyl thioglucoside micelles
    • Brackman JC, van Os NM, Engberts. JBFN. Polymer-nonionic micelle complexation. Formation of poly(propyleneoxide)-complex n-octyl thioglucoside micelles. Langmuir 1988; 4: 1266-1269.
    • (1988) Langmuir , vol.4 , pp. 1266-1269
    • Brackman, J.C.1    van Os, N.M.2    Engberts, J.B.F.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.