메뉴 건너뛰기




Volumn 5, Issue 7, 1999, Pages 298-305

Effect of amino acid substitution in amphiphilic α-helical peptides on peptide-phospholipid membrane interaction

Author keywords

Amphiphilic peptide; Antibacterial activity; Circular dichroism; Hemolytic activity; Membrane perturbation

Indexed keywords

AMINO ACID; AMPHOPHILE; PEPTIDE; PHOSPHOLIPID;

EID: 0032766379     PISSN: 10752617     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1099-1387(199907)5:7<298::AID-PSC197>3.0.CO;2-5     Document Type: Article
Times cited : (11)

References (27)
  • 2
    • 0030721013 scopus 로고    scopus 로고
    • Influence of the angle subtended by the positive charged helix face on the membrane activity of amphipathic, antibacterial peptides
    • Wieprecht T, Dathe M, Epand RM, Beyerman M, Krause E, Maloy WL, MacDonald DL, Bienert M. Influence of the angle subtended by the positive charged helix face on the membrane activity of amphipathic, antibacterial peptides. Biochemistry 1997; 36: 12869-12880.
    • (1997) Biochemistry , vol.36 , pp. 12869-12880
    • Wieprecht, T.1    Dathe, M.2    Epand, R.M.3    Beyerman, M.4    Krause, E.5    Maloy, W.L.6    MacDonald, D.L.7    Bienert, M.8
  • 3
    • 0028876215 scopus 로고
    • Enhanced membrane-perturbing activities of bundled amphiphilic α-helix polypeptides on interaction with phospholipid bilayer
    • Sakamoto S, Mihara H, Matsuo E, Niidome T, Anzai K, Kirino Y, Aoyagi H. Enhanced membrane-perturbing activities of bundled amphiphilic α-helix polypeptides on interaction with phospholipid bilayer. Bull Chem Soc Jpn 1995; 68: 2931-2939.
    • (1995) Bull Chem Soc Jpn , vol.68 , pp. 2931-2939
    • Sakamoto, S.1    Mihara, H.2    Matsuo, E.3    Niidome, T.4    Anzai, K.5    Kirino, Y.6    Aoyagi, H.7
  • 4
    • 0028339191 scopus 로고
    • Cell-lytic and antibacterial peptides that act by perturbing the barrier function of membranes: Facets of their conformational features, structure-function correlations and membrane-perturbing abilities
    • Saberwal G, Nararaj R. Cell-lytic and antibacterial peptides that act by perturbing the barrier function of membranes: facets of their conformational features, structure-function correlations and membrane-perturbing abilities. Biochim Biophys Acta 1994; 1197: 109-131.
    • (1994) Biochim Biophys Acta , vol.1197 , pp. 109-131
    • Saberwal, G.1    Nararaj, R.2
  • 5
    • 0030041468 scopus 로고    scopus 로고
    • Structural study of the interaction between the SIV fusion peptide and model membranes
    • Colotto A, Martin I, Ruysschaert J-M, Sen A, Hui SW, Epand RM. Structural study of the interaction between the SIV fusion peptide and model membranes. Biochemistry 1996; 35: 980-989.
    • (1996) Biochemistry , vol.35 , pp. 980-989
    • Colotto, A.1    Martin, I.2    Ruysschaert, J.-M.3    Sen, A.4    Hui, S.W.5    Epand, R.M.6
  • 6
    • 0029915994 scopus 로고    scopus 로고
    • Interaction of fusogenic synthetic peptide with phospholipid bilayers: Orientation of the peptide α-helix and binding isotherm
    • Ishiguro R, Matsumoto M, Takahashi S. Interaction of fusogenic synthetic peptide with phospholipid bilayers: orientation of the peptide α-helix and binding isotherm. Biochemistry 1996; 35: 4976-4983.
    • (1996) Biochemistry , vol.35 , pp. 4976-4983
    • Ishiguro, R.1    Matsumoto, M.2    Takahashi, S.3
  • 7
    • 0039196189 scopus 로고    scopus 로고
    • Membrane fusion induced by 11-mer anionic and cationic peptides: A structure-function study
    • Pécheur E-I, Martin I, Ruysschaert J-M, Bienvenüe A, Hoekstra D. Membrane fusion induced by 11-mer anionic and cationic peptides: a structure-function study. Biochemistry 1998; 37: 2361-2371.
    • (1998) Biochemistry , vol.37 , pp. 2361-2371
    • Pécheur, E.-I.1    Martin, I.2    Ruysschaert, J.-M.3    Bienvenüe, A.4    Hoekstra, D.5
  • 8
    • 0031039956 scopus 로고    scopus 로고
    • Peptide antibiotics
    • Hancock RE. Peptide antibiotics. Lancet 1997; 349: 418-422.
    • (1997) Lancet , vol.349 , pp. 418-422
    • Hancock, R.E.1
  • 9
    • 0031451521 scopus 로고    scopus 로고
    • Design of synthetic antimicrobial peptides based on sequence analogy and amphipathicity
    • Tossi A, Tarantio C, Romeo D. Design of synthetic antimicrobial peptides based on sequence analogy and amphipathicity. Eur J Biochem 1997; 250, 594-558.
    • (1997) Eur J Biochem , vol.250 , pp. 594-1558
    • Tossi, A.1    Tarantio, C.2    Romeo, D.3
  • 10
    • 0027043261 scopus 로고
    • Design of model amphipathic peptides having potent antimicrobial activities
    • Blondelle SE, Houghten RA. Design of model amphipathic peptides having potent antimicrobial activities. Biochemistry 1992; 31: 12688-12694.
    • (1992) Biochemistry , vol.31 , pp. 12688-12694
    • Blondelle, S.E.1    Houghten, R.A.2
  • 11
    • 0029065501 scopus 로고    scopus 로고
    • Translation of a channel-forming antimicrobial peptide, magainin 2, across lipid bilayers by forming a pore
    • Matsuzaki K, Murase O, Fujii N, Miyajima K. Translation of a channel-forming antimicrobial peptide, magainin 2, across lipid bilayers by forming a pore. Biochemistry 1996; 34: 6521-6526.
    • (1996) Biochemistry , vol.34 , pp. 6521-6526
    • Matsuzaki, K.1    Murase, O.2    Fujii, N.3    Miyajima, K.4
  • 12
    • 0029870676 scopus 로고    scopus 로고
    • Peptide models for membrane channels
    • Marsh D. Peptide models for membrane channels. Biochem J 1996; 315: 345-361.
    • (1996) Biochem J , vol.315 , pp. 345-361
    • Marsh, D.1
  • 14
    • 0030867021 scopus 로고    scopus 로고
    • Assembly of the four individual helices corresponding to the transmembrane segments (S4 in repeat I-IV) of the sodium channel
    • Futaki S, Aoki M, Fukuda M, Kondo F, Niwa M, Kitagawa K. Assembly of the four individual helices corresponding to the transmembrane segments (S4 in repeat I-IV) of the sodium channel. Tetrahedron Lett 1997; 38: 7071-7074.
    • (1997) Tetrahedron Lett , vol.38 , pp. 7071-7074
    • Futaki, S.1    Aoki, M.2    Fukuda, M.3    Kondo, F.4    Niwa, M.5    Kitagawa, K.6
  • 15
    • 0029153215 scopus 로고
    • Peptides in membranes: Helicity and hydrophobicity
    • Deber CM, Li S-C. Peptides in membranes: helicity and hydrophobicity. Biopolymers 1995; 37: 295-318.
    • (1995) Biopolymers , vol.37 , pp. 295-318
    • Deber, C.M.1    Li, S.-C.2
  • 16
    • 0030249150 scopus 로고    scopus 로고
    • Threshold hydrophobicity dictates helical conformtions of peptides in membrane environments
    • Liu LP, Li S-C, Goto NK, Deber CM. Threshold hydrophobicity dictates helical conformtions of peptides in membrane environments. Biopolymers 1996; 39: 465-470.
    • (1996) Biopolymers , vol.39 , pp. 465-470
    • Liu, L.P.1    Li, S.-C.2    Goto, N.K.3    Deber, C.M.4
  • 17
    • 0023404610 scopus 로고
    • Proline-induced constraints in α-helices
    • Piela L, Nemethy G, Scheraga HA. Proline-induced constraints in α-helices. Biopolymers 1987; 26: 1587-1600.
    • (1987) Biopolymers , vol.26 , pp. 1587-1600
    • Piela, L.1    Nemethy, G.2    Scheraga, H.A.3
  • 18
    • 0022993071 scopus 로고
    • Relationship between antimicrobial activity and amphiphilic property of basic model peptides
    • Lee S, Mihara H, Aoyagi H, Kato T, Izumiya N, Yamasaki N. Relationship between antimicrobial activity and amphiphilic property of basic model peptides. Biochim Biophys Acta 1986; 862: 211-219.
    • (1986) Biochim Biophys Acta , vol.862 , pp. 211-219
    • Lee, S.1    Mihara, H.2    Aoyagi, H.3    Kato, T.4    Izumiya, N.5    Yamasaki, N.6
  • 19
    • 0023108007 scopus 로고
    • Design and synthesis of amphiphilic basic peptides with antibacterial activity and their interaction with model membrane
    • Mihara H, Kanmera T, Yoshida M, Lee S, Aoyagi H, Kato T, Izumiya N. Design and synthesis of amphiphilic basic peptides with antibacterial activity and their interaction with model membrane. Bull Chem Soc Jpn 1987; 60: 697-706.
    • (1987) Bull Chem Soc Jpn , vol.60 , pp. 697-706
    • Mihara, H.1    Kanmera, T.2    Yoshida, M.3    Lee, S.4    Aoyagi, H.5    Kato, T.6    Izumiya, N.7
  • 20
    • 0031890615 scopus 로고    scopus 로고
    • Interaction of α-helical peptides with phospholipid membrane: Effect of chain length and hydrophobicity of peptide
    • Ohmori N, Niidome T, Hatakeyama T, Mihara H, Aoyagi H. Interaction of α-helical peptides with phospholipid membrane: effect of chain length and hydrophobicity of peptide. J Peptide Res 1998; 51: 103-109.
    • (1998) J Peptide Res , vol.51 , pp. 103-109
    • Ohmori, N.1    Niidome, T.2    Hatakeyama, T.3    Mihara, H.4    Aoyagi, H.5
  • 21
    • 0007686844 scopus 로고
    • Effect of proline in basic and α-helical amphipathic peptides on acidic liposomes and their antimicrobial activity
    • Lee S, Park NG, Kato T, Aoyagi H, Kato T. Effect of proline in basic and α-helical amphipathic peptides on acidic liposomes and their antimicrobial activity. Chem Lett 1989, 599-602.
    • (1989) Chem Lett , pp. 599-602
    • Lee, S.1    Park, N.G.2    Kato, T.3    Aoyagi, H.4    Kato, T.5
  • 22
    • 0026254055 scopus 로고
    • Parameters of helix-coil transition theory for alanine-based peptides of varying chain lengths in water
    • Scholtz JM, Qian H, York EJ, Stewart JM, Baldwin RL. Parameters of helix-coil transition theory for alanine-based peptides of varying chain lengths in water. Biopolymers 1991; 31: 1463-1470.
    • (1991) Biopolymers , vol.31 , pp. 1463-1470
    • Scholtz, J.M.1    Qian, H.2    York, E.J.3    Stewart, J.M.4    Baldwin, R.L.5
  • 23
    • 0021152462 scopus 로고
    • Three-dimensional structure of membrane and surface proteins
    • Eisenberg D. Three-dimensional structure of membrane and surface proteins. Annu Rev Biochem 1984; 53: 595-623.
    • (1984) Annu Rev Biochem , vol.53 , pp. 595-623
    • Eisenberg, D.1
  • 24
    • 0017868338 scopus 로고
    • Empirical properties of protein conformation
    • Chou PY, Fasman GD. Empirical properties of protein conformation. Annu Rev Biochem 1978; 47: 251-276.
    • (1978) Annu Rev Biochem , vol.47 , pp. 251-276
    • Chou, P.Y.1    Fasman, G.D.2
  • 25
    • 0021911741 scopus 로고
    • Bombolitins, a new class of mast cell degranulating peptides from the venom of the bumblebee Megabombus pennsylvanicus
    • Argiolas A, Pisano JJ. Bombolitins, a new class of mast cell degranulating peptides from the venom of the bumblebee Megabombus pennsylvanicus. J Biol Chem 1985; 260: 1437-1444.
    • (1985) J Biol Chem , vol.260 , pp. 1437-1444
    • Argiolas, A.1    Pisano, J.J.2
  • 27
    • 10144229398 scopus 로고    scopus 로고
    • Peptide helicity and membrane surface charge modulate the balance of electrostatic and hydrophobic interactions with lipid bilayers and biological membranes
    • Dathe M, Shumann M, Wieprecht T, Winkler A, Beyerman M, Krause E, Matsuzaki K, Murase O, Bienert M. Peptide helicity and membrane surface charge modulate the balance of electrostatic and hydrophobic interactions with lipid bilayers and biological membranes. Biochemistry 1996; 35: 12612-12622.
    • (1996) Biochemistry , vol.35 , pp. 12612-12622
    • Dathe, M.1    Shumann, M.2    Wieprecht, T.3    Winkler, A.4    Beyerman, M.5    Krause, E.6    Matsuzaki, K.7    Murase, O.8    Bienert, M.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.