Abstract
Membrane-active peptides exhibit antimicrobial, channel-forming and transport activities and have therefore early on been interesting targets for biophysical investigations. When the peptide-lipid interactions are studied a dynamic view emerges in which the peptides change conformation upon membrane insertion, can adopt a variety of topologies and change the macroscopic phase properties of the membrane locally or globally. Interestingly several proteins have been identified that also interact with the membrane in a dynamic fashion and where the lessons learned from peptides may add to our understanding of the ways these proteins function.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Tusnady GE, Dosztanyi Z, Simon I. Transmembrane proteins in the protein data bank: identification and classification. Bioinformatics 2004; 20:2964–2972.
Raman P, Cherezov V, Caffrey M. The membrane protein data bank. Cell Mol Life Sci 2006; 63:36–51.
Bechinger B. Structure and functions of channel-forming polypeptides: magainins, cecropins, melittin and alamethicin. J Membrane Biol 1997; 156:197–211.
Lear JD, Wasserman ZR, DeGrado WF. Synthetic amphiphilic peptide models for protein ion channels. Science 1988; 240:1177–1181.
Bechinger B. Towards membrane protein design: pH dependent topology of histidine-containing polypeptides. J Mol Biol 1996; 263:768–775.
Killian JA, Salemink I, de Planque MRR et al. Induction of nonbilayer structures in diacylphosphatidylcholine model membranes by transmembrane a-helical peptides: Importance of hydrophobic mismatch and propose role of tryptophans. Biochemistry 1996; 35:1037–1045.
Hong M. Oligomeric structure, dynamics and orientation of membrane proteins from solid-state NMR. Structure 2006; 14:1731–1740.
Salnikov ES, Friedrich H, Li X et al. Structure and alignment of the membrane-associated peptaibols ampullosporin A and alamethicin by oriented 15N and 31P solid-state NMR spectroscopy. Biophys J 2009; 96:86–100.
Leitgeb B, Szekeres A, Manczinger L et al. The history of alamethicin: a review of the most extensively studied peptaibol. Chem Biodivers 2007; 4:1027–1051.
Sansom MS. Alamethicin and related peptaibols—model ion channels. Eur Biophys J 1993; 22:105–124.
Thogersen L, Schiott B, Vosegaard T et al. Peptide aggregation and pore formation in a lipid bilayer: a combined coarse-grained and all atom molecular dynamics study. Biophys J 2008; 95:4337–4347.
Unwin N. Refined structure of the nicotinic acetylcholine receptor at 4A resolution. J Mol Biol 2005; 346:967–989.
Oxenoid K, Rice AJ, Chou JJ. Comparing the structure and dynamics of phospholamban pentamer in its unphosphorylated and pseudo-phosphorylated states. Protein Sci 2007; 16:1977–1983.
Traaseth NJ, Verardi R, Torgersen KD et al. Spectroscopic validation of the pentameric structure of phospholamban. Proc Natl Acad Sci USA 2007; 104:14676–14681.
Long SB, Tao X, Campbell EB et al. Atomic structure of a voltage-dependent K+ channel in a lipid membrane-like environment. Nature 2007; 450:376–382.
Schnell JR, Chou JJ. Structure and mechanism of the M2 proton channel of influenza A virus. Nature 2008; 451:591–595.
Stouffer AL, Acharya R, Salom D et al. Structural basis for the function and inhibition of an influenza virus proton channel. Nature 2008; 451:596–599.
Yee A, Szymczyna B, O’Neil JD. Backbone dynamics of detergent-solubilized alamethicin from amide hydrogen exchange measurements. Biochemistry 1999; 38:6489–6498.
Jacob J, Duclohier H, Cafiso DS. The role of proline and glycine in determining the backbone flexibility of a channel-forming peptide. Biophys J 1999; 76:1367–1376.
Franklin JC, Ellena JF, Jayasinghe S et al. Structure of micelle-associated alamethicin from 1H NMR. Evidence for conformational heterogeneity in a voltage-gated peptide. Biochemistry 1994; 33:4036–4045.
North CL, Barranger-Mathys M, Cafiso DS. Membrane orientation of the N-terminal segment of alamethicin determined by solid-state 15N NMR. Biophys J 1995; 69:2392–2397.
Bechinger B, Skladnev DA, Ogrel A et al 15N and 31P solid-state NMR investigations on the orientation of zervamicin II and alamethicin in phosphatidylcholine membranes. Biochemistry 2001; 40:9428–9437.
Bak M, Bywater RP, Hohwy M et al. Conformation of alamethicin in oriented phospholipid bilayers determined by N-15 solid-state nuclear magnetic resonance. Biophys J 2001; 81:1684–1698.
Sansom MSP. The biophysics of peptide models of ion channels. Prog Biophys Molec Biol 1991; 55:139–235.
Huang HW. Action of antimicrobial peptides: Two-state model. Biochemistry 2000; 39:8347–8352.
Okazaki T, Sakoh M, Nagaoka Y et al. Ion channels of alamethicin dimer N-terminally linked by disulfide bond. Biophys J 2003; 85:267–273.
Sudheendra US, Bechinger B. Topological equilibria of ion channel peptides in oriented lipid bilayers revealed by 15N solid-state NMR spectroscopy. Biochemistry 2005; 44:12120–12127.
Salnikov ES, De Zotti M, Formaggio F et al. Alamethicin topology in phospholipid membranes by oriented solid-state NMR and EPR spectroscopies: A comparison. J Phys Chem B 2009; 113:3034–3042.
Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 2002; 415:389–395.
Boman HG. Antibacterial peptides: basic facts and emerging concepts. J Intern Med 2003; 254:197–215.
Bechinger B. The structure, dynamics and orientation of antimicrobial peptides in membranes by solid-state NMR spectroscopy. Biochim Biophys Acta 1999; 1462:157–183.
Shai Y. Mode of action of membrane active antimicrobial peptides. Biopolymers 2002; 66:236–248.
Brogden KA. Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria? Nat Rev Microbiol 2005; 3:238–250.
Matsuzaki K, Murase O, Tokuda H et al. Orientational and Aggregational States of Magainin 2 in Phospholipid Bilayers. Biochemistry 1994; 33:3342–3349.
Salnikov ES, Mason AJ, Bechinger B. Membrane order perturbation in the presence of antimicrobial peptides by 2H solid-state NMR spectroscopy. Biochimie 2009; 91:734–743.
Ludtke S, He K, Huang H. Membrane thinning caused by magainin 2. Biochemistry 1995; 34:16764–1679.
Gregory SM, Cavenaugh A, Journigan V et al. A quantitative model for the all-or-none permeabilization of phospholipid vesicles by the antimicrobial peptide cecropin A. Biophys J 2008; 94:1667–1680.
Bechinger B. Rationalizing the membrane interactions of cationic amphipathic antimicrobial peptides by their molecular shape. Current Opinion in Colloid and Interface Science, Surfactants (in press) 2009.
Mozsolits H, Wirth HJ, Werkmeister J et al. Analysis of antimicrobial peptide interactions with hybrid bilayer membrane systems using surface plasmon resonance. Biochim Biophys Acta 2001; 1512:64–76.
Papo N, Shai Y. Exploring peptide membrane interaction using surface plasmon resonance: differentiation between pore formation versus membrane disruption by lytic peptides. Biochemistry 2003; 42:458–466.
Wieprecht T, Beyermann M, Seelig J. Binding of antibacterial magainin peptides to electrically neutral membranes: Thermodynamics and structure. Biochemistry 1999; 38:10377–10378.
Wenk M, Seelig J. Magainin 2 amide interaction with lipid membranes: Calorimetric detection of peptide binding and pore formation. Biochemistry 1998; 37:3909–3916.
Vogt TCB, Bechinger B. The interactions of histidine-containing amphipathic helical peptide antibiotics with lipid bilayers: The effects of charges and pH. J Biol Chem 1999; 274:29115–29121.
Wieprecht T, Apostolov O, Beyermann M et al. Membrane binding and pore formation of the antibacterial peptide PGLa: thermodynamic and mechanistic aspects. Biochemistry 2000; 39:442–452.
Dathe M, Nikolenko H, Meyer J et al. Optimization of the antimicrobial activity of magainin peptides by modification of charge. FEBS Lett 2001; 501:146–150.
Mason AJ, Martinez A, Glaubitz C et al. The antibiotic and DNA-transfecting peptide LAH4 selectively associates with and disorders, anionic lipids in mixed membranes. FASEB J 2006; 20:320–322.
Chen FY, Lee MT, Huang HW. Evidence for membrane thinning effect as the mechanism for Peptide-induced pore formation. Biophys J 2003; 84:3751–3758.
Mecke A, Lee DK, Ramamoorthy A et al. Membrane thinning due to antimicrobial peptide binding: an atomic force microscopy study of MSI-78 in lipid bilayers. Biophys J 2005; 89:4043–4050.
Bechinger B, Lohner K. Detergent-like action of linear cationic membrane-active antibiotic peptides. Biochim Biophys Acta 2006; 1758:1529–1539.
Dvinskikh S, Durr U, Yamamoto K et al. A high-resolution solid-state NMR approach for the structural studies of bicelles. J Am Chem Soc 2006; 128:6326–6327.
Mason AJ, Bechinger B. Zwitterionic lipids and sterols modulate antimicrobial peptide-membrane interactions. Biophys J 2007; 93:4289–4299.
Dufourc EJ, Smith IC, Dufourcq J. Molecular details of melittin-induced lysis of phospholipid membranes as revealed by deuterium and phosphorus NMR. Biochemistry 1986; 25:6448–6455.
Hallock KJ, Lee DK, Omnaas J et al. Membrane composition determines pardaxin’s mechanism of lipid bilayer disruption. Biophys J 2002; 83:1004–1013.
Bechinger B. Detergent-like properties of magainin antibiotic peptides: A 31P solid-state NMR study. Biochim Biophys Acta 2005; 1712:101–108.
Batenburg AM, van Esch JH, de Kruijff B. Melittin-induced changes of the macroscopic structure of phosphatidylethanolamines. Biochemistry 1988; 27:2324–2331.
Zakharov SD, Lindeberg M, Griko Y et al. Membrane-bound state of the colicin E1 channel domain as an extended two-dimensional helical array. Proc Natl Acad Sci USA 1998; 95:4282–4287.
Stroud RM, Reiling K, Wiener M et al. Ion-channel-forming colicins. Curr Opin Struct Biol 1998; 8:525–533.
Lakey JH, Slatin SL. Pore-forming colicins and their relatives. Curr Top Microbiol Immunol 2001; 257:131–161.
Zakharov SD, Cramer WA. Colicin crystal structures: pathways and mechanisms for colicin insertion into membranes. Biochim Biophys Acta 2002; 1565:333–346.
Petros AM, Olejniczak ET, Fesik SW. Structural biology of the Bcl-2 family of proteins. Biochim Biophys Acta 2004; 1644:83–94.
Pattus F, Massotte D, Wilmsen HU et al. Colicins: prokaryotic killer-pores. Experientia 1990; 46:180–192.
Sathish HA, Cusan M, Aisenbrey C et al. Guanidine hydrochloride induced equilibrium unfolding studies of colicin B and its channel-forming fragment. Biochemistry 2002; 41:5340–5347.
Aisenbrey C, Sudheendra US, Ridley H et al. Helix orientations in membrane-associated Bcl-XL determined by 15N solid-state NMR spectroscopy. Eur Biophys J 2007; 36:451–460.
Losonczi JA, Olejniczak ET, Betz SF et al. NMR studies of the anti-apoptotic protein Bcl-x(L) in micelles. Biochemistry 2000; 39:11024–11033.
Kienker PK, Qiu X, Slatin SL et al. Transmembrane insertion of the colicin Ia hydrophobic hairpin. J Membrane Biol 1997; 157:27–37.
Aisenbrey C, Cusan M, Lambotte S et al. Specific isotope labeling of colicin E1 and B channel domains for membrane topological analysis by oriented solid-state NMR spectroscopy. Chem Bio Chem 2008; 9:944–951.
Malenbaum SE, Collier RJ, London E. Membrane topography of the T domain of diphtheria toxin probed with single tryptophan mutants. Biochemistry 1998; 37:17915–17922.
Chenal A, Prongidi-Fix L, Perier A et al. Deciphering membrane insertion of the diphtheria toxin T domain by specular neutron reflectometry and solid-state NMR spectroscopy. J Mol Biol 2009; 391:872–883
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2010 Landes Bioscience and Springer Science+Business Media
About this chapter
Cite this chapter
Bechinger, B. (2010). Membrane Association and Pore Formation by Alpha-Helical Peptides. In: Anderluh, G., Lakey, J. (eds) Proteins Membrane Binding and Pore Formation. Advances in Experimental Medicine and Biology, vol 677. Springer, New York, NY. https://doi.org/10.1007/978-1-4419-6327-7_3
Download citation
DOI: https://doi.org/10.1007/978-1-4419-6327-7_3
Publisher Name: Springer, New York, NY
Print ISBN: 978-1-4419-6326-0
Online ISBN: 978-1-4419-6327-7
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)