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Volumn 47, Issue 32, 2008, Pages 8250-8252

Dissecting the membrane binding and insertion kinetics of a pHLIP peptide

Author keywords

[No Author keywords available]

Indexed keywords

AMINES; ASSOCIATION REACTIONS; LIPID BILAYERS;

EID: 49449096024     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi801103x     Document Type: Article
Times cited : (21)

References (18)
  • 1
    • 0030723767 scopus 로고    scopus 로고
    • Spontaneous, pH-dependent membrane insertion of a transbilayer α helix
    • Hunt, J. F., Rath, P., Rothschild, K. J., and Engelman, D. M. (1997) Spontaneous, pH-dependent membrane insertion of a transbilayer α helix. Biochemistry 36, 15177-15192.
    • (1997) Biochemistry , vol.36 , pp. 15177-15192
    • Hunt, J.F.1    Rath, P.2    Rothschild, K.J.3    Engelman, D.M.4
  • 2
    • 33646272211 scopus 로고    scopus 로고
    • Translocation of molecules into cells by pH-dependent insertion of a transmembrane helix
    • Reshetnyak, Y. K., Andreev, O. A., Lehnert, U., and Engelman, D. M. (2006) Translocation of molecules into cells by pH-dependent insertion of a transmembrane helix. Proc. Natl. Acad. Sci. U.S.A. 103, 6460-6465.
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 6460-6465
    • Reshetnyak, Y.K.1    Andreev, O.A.2    Lehnert, U.3    Engelman, D.M.4
  • 4
    • 34848885103 scopus 로고    scopus 로고
    • A monomeric membrane peptide that lives in three worlds: In solution, attached to, and inserted across lipid bilayers
    • Reshetnyak, Y. K., Segala, M., Andreev, O. A., and Engelman, D. M. (2007) A monomeric membrane peptide that lives in three worlds: In solution, attached to, and inserted across lipid bilayers. Biophys. J. 93, 2363-2372.
    • (2007) Biophys. J , vol.93 , pp. 2363-2372
    • Reshetnyak, Y.K.1    Segala, M.2    Andreev, O.A.3    Engelman, D.M.4
  • 5
    • 46749116786 scopus 로고    scopus 로고
    • Bilayer interactions of pHLIP, a peptide that can deliver drugs and target tumors
    • Zoonens, M. A., Reshetnyak, Y. K., and Engelman, D. M. (2008) Bilayer interactions of pHLIP, a peptide that can deliver drugs and target tumors. Biophys. J. 95, 225-235.
    • (2008) Biophys. J , vol.95 , pp. 225-235
    • Zoonens, M.A.1    Reshetnyak, Y.K.2    Engelman, D.M.3
  • 6
    • 49449116983 scopus 로고    scopus 로고
    • POPC (purchased from Avanti Polar Lipids) vesicles (200 nm) were prepared using an extrusion method, the details of which are described in ref 8.
    • POPC (purchased from Avanti Polar Lipids) vesicles (200 nm) were prepared using an extrusion method, the details of which are described in ref 8.
  • 7
    • 33646421139 scopus 로고    scopus 로고
    • Probing the kinetics of membrane-mediated helix folding
    • Tucker, M. J., Tang, J., and Gai, F. (2006) Probing the kinetics of membrane-mediated helix folding. J. Phys. Chem. B 110, 8105-8109.
    • (2006) J. Phys. Chem. B , vol.110 , pp. 8105-8109
    • Tucker, M.J.1    Tang, J.2    Gai, F.3
  • 8
    • 36849087359 scopus 로고    scopus 로고
    • Role of helix nucleation in the kinetics of binding of mastoparan X to phospholipid bilayers
    • Tang, J., Signarvic, R. S., DeGrado, W. F., and Gai, F. (2007) Role of helix nucleation in the kinetics of binding of mastoparan X to phospholipid bilayers. Biochemistry 46, 13856-13863.
    • (2007) Biochemistry , vol.46 , pp. 13856-13863
    • Tang, J.1    Signarvic, R.S.2    DeGrado, W.F.3    Gai, F.4
  • 10
    • 40149084042 scopus 로고    scopus 로고
    • Small changes in the primary structure of transportan 10 alter the thermodynamics and kinetics of its interaction with phospholipid vesicles
    • Yandek, L. E., Pokorny, A., and Almeida, P. F. F. (2008) Small changes in the primary structure of transportan 10 alter the thermodynamics and kinetics of its interaction with phospholipid vesicles. Biochemistry 47, 3051-3060.
    • (2008) Biochemistry , vol.47 , pp. 3051-3060
    • Yandek, L.E.1    Pokorny, A.2    Almeida, P.F.F.3
  • 11
    • 0029764221 scopus 로고    scopus 로고
    • Time resolution of binding and membrane insertion of a mitochondrial signal peptide: Correlation with structural changes and evidence for cooperativity
    • Golding, C., Senior, S., Wilson, M. T., and O'Shea, P. (1996) Time resolution of binding and membrane insertion of a mitochondrial signal peptide: Correlation with structural changes and evidence for cooperativity. Biochemistry 35, 10931-10937.
    • (1996) Biochemistry , vol.35 , pp. 10931-10937
    • Golding, C.1    Senior, S.2    Wilson, M.T.3    O'Shea, P.4
  • 12
    • 7744240086 scopus 로고    scopus 로고
    • Influence of the lipid composition on the kinetics of concerted insertion and folding of melittin in bilayers
    • Constantinescu, I., and Lafleur, M. (2004) Influence of the lipid composition on the kinetics of concerted insertion and folding of melittin in bilayers. Biochim. Biophys. Acta 1676, 26-37.
    • (2004) Biochim. Biophys. Acta , vol.1676 , pp. 26-37
    • Constantinescu, I.1    Lafleur, M.2
  • 13
    • 0036306814 scopus 로고    scopus 로고
    • The activation energy for insertion of transmembrane α-helices is dependent on membrane composition
    • Meijberg, W., and Booth, P. J. (2002) The activation energy for insertion of transmembrane α-helices is dependent on membrane composition. J. Mol. Biol. 319, 839-853.
    • (2002) J. Mol. Biol , vol.319 , pp. 839-853
    • Meijberg, W.1    Booth, P.J.2
  • 14
    • 1942425119 scopus 로고    scopus 로고
    • A new method for determining the local environment and orientation of individual side chains of membrane-binding peptides
    • Tucker, M. J., Getahun, Z., Nanda, V., DeGrado, W. F., and Gai, F. (2004) A new method for determining the local environment and orientation of individual side chains of membrane-binding peptides. J. Am. Chem. Soc. 126, 5078-5079.
    • (2004) J. Am. Chem. Soc , vol.126 , pp. 5078-5079
    • Tucker, M.J.1    Getahun, Z.2    Nanda, V.3    DeGrado, W.F.4    Gai, F.5
  • 15
    • 0034127327 scopus 로고    scopus 로고
    • Fast events in protein folding: Structural volume changes accompanying the early events in the N→I transition of apomyoglobin induced by ultrafast pH jump
    • Abbruzzetti, S., Crema, E., Masino, L., Vecli, A., Viappiani, C., Small, J. R., Libertini, L. J., and Small, E. W. (2000) Fast events in protein folding: Structural volume changes accompanying the early events in the N→I transition of apomyoglobin induced by ultrafast pH jump. Biophys. J. 78, 405-415.
    • (2000) Biophys. J , vol.78 , pp. 405-415
    • Abbruzzetti, S.1    Crema, E.2    Masino, L.3    Vecli, A.4    Viappiani, C.5    Small, J.R.6    Libertini, L.J.7    Small, E.W.8
  • 16
    • 0035132984 scopus 로고    scopus 로고
    • Voltage-dependent insertion of alamethicin at phospholipid/water and octane/water interfaces
    • Tieleman, D. P., Berendsen, H. J. C., and Sansom, M. S. P. (2001) Voltage-dependent insertion of alamethicin at phospholipid/water and octane/water interfaces. Biophys. J. 80, 331-346.
    • (2001) Biophys. J , vol.80 , pp. 331-346
    • Tieleman, D.P.1    Berendsen, H.J.C.2    Sansom, M.S.P.3
  • 17
    • 18744403982 scopus 로고    scopus 로고
    • Interfacial folding and membrane insertion of designed peptides studied by molecular dynamics simulations
    • Im, W., and Brooks, C. L. (2005) Interfacial folding and membrane insertion of designed peptides studied by molecular dynamics simulations. Proc. Natl. Acad. Sci. U.S.A. 102, 6771-6776.
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 6771-6776
    • Im, W.1    Brooks, C.L.2
  • 18
    • 38049156027 scopus 로고    scopus 로고
    • Molecular dynamics simulations suggest a mechanism for translocation of the HIV-1 TAT peptide across lipid membranes
    • Herce, H. D., and Garcia, A. E. (2007) Molecular dynamics simulations suggest a mechanism for translocation of the HIV-1 TAT peptide across lipid membranes. Proc. Natl. Acad. Sci. U.S.A. 104, 20805-20810.
    • (2007) Proc. Natl. Acad. Sci. U.S.A , vol.104 , pp. 20805-20810
    • Herce, H.D.1    Garcia, A.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.