The Polymorphic Nature of Membrane-Active Peptides from Biophysical and Structural Investigations

被引:22
作者
Bechinger, Burkhard [1 ]
Aisenbrey, Christopher [1 ]
机构
[1] Univ Strasbourg, CNRS, UMR7177, Inst Chim,Fac Chim, F-67070 Strasbourg, France
关键词
Alamethicin; cecropin; hydrophobic mismatch; membrane topology; solid-state NMR; supported bilayers; SOLID-STATE NMR; CELL-PENETRATING PEPTIDES; HISTIDINE-RICH PEPTIDES; NUCLEAR-MAGNETIC-RESONANCE; SODIUM DODECYL-SULFATE; MAGAININ; AMIDE; ANTIMICROBIAL PEPTIDES; LIPID-BILAYERS; ANTIBACTERIAL PEPTIDES; ANTIBIOTIC PEPTIDES;
D O I
10.2174/138920312804142093
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Membrane-active peptides exhibit a wide variety of biological functions including pore formation, signaling and antimicrobial activities. They are also capable of transporting large cargo such as proteins or nucleic acids across cell membranes. This review summarizes biophysical and structural investigations on hydrophobic, amphipathic and heavily charged peptides that reveal a very dynamic view on their membrane interactions. Individual peptides are able to adopt a variety of different conformations and topology and at the same time exhibit multimodal functionalities. Examples discussed in this paper include peptaibols, magainins, cell penetrating peptides and designed histidine-rich sequences with potent antimicrobial and nucleic acid transfection activities.
引用
收藏
页码:602 / 610
页数:9
相关论文
共 102 条
[31]  
García-Olmedo F, 1998, BIOPOLYMERS, V47, P479, DOI 10.1002/(SICI)1097-0282(1998)47:6<479::AID-BIP6>3.0.CO
[32]  
2-K
[33]   NMR Structures of the Histidine-Rich Peptide LAH4 in Micellar Environments: Membrane Insertion, pH-Dependent Mode of Antimicrobial Action, and DNA Transfection [J].
Georgescu, Julia ;
Munhoz, Victor H. O. ;
Bechinger, Burkhard .
BIOPHYSICAL JOURNAL, 2010, 99 (08) :2507-2515
[34]   Two-dimensional H-1 NMR experiments show that the 23-residue magainin antibiotic peptide is an alpha-helix in dodecylphosphocholine micelles, sodium dodecylsulfate micelles, and trifluoroethanol/water solution [J].
Gesell, J ;
Zasloff, M ;
Opella, SJ .
JOURNAL OF BIOMOLECULAR NMR, 1997, 9 (02) :127-135
[35]   Concentration-dependent realignment of the antimicrobial peptide PGLa in lipid membranes observed by solid-state 19F-NMR [J].
Glaser, RW ;
Sachse, C ;
Dürr, UHN ;
Wadhwani, P ;
Afonin, S ;
Strandberg, E ;
Ulrich, AS .
BIOPHYSICAL JOURNAL, 2005, 88 (05) :3392-3397
[36]   Twenty years of cell-penetrating peptides: from molecular mechanisms to therapeutics [J].
Heitz, Frederic ;
Morris, May Catherine ;
Divita, Gilles .
BRITISH JOURNAL OF PHARMACOLOGY, 2009, 157 (02) :195-206
[37]   Cell-penetrating peptides and antimicrobial peptides: how different are they? [J].
Henriques, Sonia Troeira ;
Melo, Manuel Nuno ;
Castanho, Miguel A. R. B. .
BIOCHEMICAL JOURNAL, 2006, 399 :1-7
[38]   Membrane surface-associated helices promote lipid interactions and cellular uptake of human calcitonin-derived cell penetrating peptides [J].
Herbig, ME ;
Weller, K ;
Krauss, U ;
Beck-Sickinger, AG ;
Merkle, HP ;
Zerbe, O .
BIOPHYSICAL JOURNAL, 2005, 89 (06) :4056-4066
[39]   Effect of divalent cations on the structure of the antibiotic daptomycin [J].
Ho, Steven W. ;
Jung, David ;
Calhoun, Jennifer R. ;
Lear, James D. ;
Okon, Mark ;
Scott, Walter R. P. ;
Hancock, Robert E. W. ;
Straus, Suzana K. .
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS, 2008, 37 (04) :421-433
[40]   Molecular mechanism of antimicrobial peptides: The origin of cooperativity [J].
Huang, Huey W. .
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, 2006, 1758 (09) :1292-1302