Surface plasmon resonance analysis of antimicrobial peptide–membrane interactions: affinity & mechanism of action

Antimicrobial peptides are being increasingly recognised as potential candidates for antibacterial drugs in the face of the rapidly emerging bacterial resistance to conventional antibiotics in recent years. However, a precise understanding of the relationship between antimicrobial peptide structure and their cytolytic function in a range of organisms is still lacking. This is a result of the complex nature of the interactions of antimicrobial peptides with the cell membrane, the mechanism of which can vary considerably between different classes of antimicrobial peptides. A wide range of biophysical techniques have been used to study the influence of a number of peptide and membrane properties on the cytolytic activity of these peptides model membrane systems. Until recently, however, very few studies had reported measurements of the affinity of antimicrobial peptides for different membrane systems mainly due to the difficulty in obtaining this information. Surface plasmon resonance (SPR) spectroscopy has recently been applied to the study of biomembrane-based systems which has allowed a real-time analysis of binding affinity and kinetics. This mini review provides an overview of the recent applications that demonstrate the potential of SPR to study the membrane interactions of antimicrobial peptides.

[1]  D. Williams,et al.  Surface plasmon resonance analysis at a supported lipid monolayer. , 1998, Biochimica et biophysica acta.

[2]  Alessandro Tossi,et al.  Amphipathic, α‐helical antimicrobial peptides , 2000 .

[3]  Dudley H. Williams,et al.  A vesicle capture sensor chip for kinetic analysis of interactions with membrane-bound receptors. , 2000, Analytical biochemistry.

[4]  S. Blondelle,et al.  Lipid-induced conformation and lipid-binding properties of cytolytic and antimicrobial peptides: determination and biological specificity. , 1999, Biochimica et biophysica acta.

[5]  W. Miller,et al.  Binding of Steroidogenic Acute Regulatory Protein to Synthetic Membranes Suggests an Active Molten Globule* , 2001, The Journal of Biological Chemistry.

[6]  M. Aguilar,et al.  Surface plasmon resonance spectroscopy: an emerging tool for the study of peptide-membrane interactions. , 2002, Biopolymers.

[7]  J. Seelig,et al.  Melittin binding to mixed phosphatidylglycerol/phosphatidylcholine membranes. , 1990, Biochemistry.

[8]  Younghoon R. Cho,et al.  SURFACE PLASMON RESONANCE ANALYSIS OF GLYCOPEPTIDE ANTIBIOTIC ACTIVITY AT A MODEL MEMBRANE SURFACE , 1997 .

[9]  C. Dempsey.  The actions of melittin on membranes. , 1990, Biochimica et biophysica acta.

[10]  N. Fujii,et al.  Molecular basis for membrane selectivity of an antimicrobial peptide, magainin 2. , 1995, Biochemistry.

[11]  B. Bechinger,et al.  Structure and Functions of Channel-Forming Peptides: Magainins, Cecropins, Melittin and Alamethicin , 1997, The Journal of Membrane Biology.

[12]  E Maier,et al.  Mechanism of interaction of different classes of cationic antimicrobial peptides with planar bilayers and with the cytoplasmic membrane of Escherichia coli. , 1999, Biochemistry.

[13]  M. Umeda,et al.  Lysenin, a Novel Sphingomyelin-specific Binding Protein* , 1998, The Journal of Biological Chemistry.

[14]  M. Lafleur,et al.  Modulation of melittin-induced lysis by surface charge density of membranes. , 1995, Biophysical journal.

[15]  A. Ghosh,et al.  Modulation of tryptophan environment in membrane-bound melittin by negatively charged phospholipids: implications in membrane organization and function. , 1997, Biochemistry.

[16]  J. Werkmeister,et al.  Analysis of antimicrobial peptide interactions with hybrid bilayer membrane systems using surface plasmon resonance. , 2001, Biochimica et biophysica acta.

[17]  Michael R. Yeaman,et al.  Mechanisms of Antimicrobial Peptide Action and Resistance , 2003, Pharmacological Reviews.

[18]  E. Zmuda,et al.  Influence of tryptophan on lipid binding of linear amphipathic cationic antimicrobial peptides. , 2003, Biochemistry.

[19]  K. Matsuzaki,et al.  Magainins as paradigm for the mode of action of pore forming polypeptides. , 1998, Biochimica et biophysica acta.

[20]  D G Myszka,et al.  Advances in surface plasmon resonance biosensor analysis. , 2000, Current opinion in biotechnology.

[21]  Vanya Gant,et al.  Structure-Function Relationship of Antibacterial Synthetic Peptides Homologous to a Helical Surface Region on Human Lactoferrin against Escherichia coli Serotype O111 , 1998, Infection and Immunity.

[22]  Niv Papo,et al.  Exploring peptide membrane interaction using surface plasmon resonance: differentiation between pore formation versus membrane disruption by lytic peptides. , 2003, Biochemistry.

[23]  R. Epand,et al.  A Novel Linear Amphipathic β-Sheet Cationic Antimicrobial Peptide with Enhanced Selectivity for Bacterial Lipids* , 2001, The Journal of Biological Chemistry.

[24]  Claus Duschl,et al.  Protein binding to supported lipid membranes: investigation of the cholera toxin-ganglioside interaction by simultaneous impedance spectroscopy and surface plasmon resonance , 1993 .

[25]  D. Williams,et al.  Binding of glycopeptide antibiotics to a model of a vancomycin-resistant bacterium. , 1999, Chemistry & biology.

[26]  W. Wang,et al.  The Dependence of Membrane Permeability by the Antibacterial Peptide Cecropin B and Its Analogs, CB-1 and CB-3, on Liposomes of Different Composition* , 1998, The Journal of Biological Chemistry.

[27]  Neta Sal-Man,et al.  Preassembly of membrane-active peptides is an important factor in their selectivity toward target cells. , 2002, Biochemistry.

[28]  A. Mor,et al.  Structural Requirements for Potent Versus Selective Cytotoxicity for Antimicrobial Dermaseptin S4 Derivatives* 210 , 2002, The Journal of Biological Chemistry.

[29]  D. Tirrell,et al.  Self-association and membrane-binding behavior of melittins containing trifluoroleucine. , 2001, Journal of the American Chemical Society.

[30]  H. G. Boman,et al.  Cell-free immunity in Cecropia , 1991 .

[31]  Y. Shai,et al.  Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides. , 1999, Biochimica et biophysica acta.

[32]  K. Matsuzaki.  Why and how are peptide-lipid interactions utilized for self-defense? Magainins and tachyplesins as archetypes. , 1999, Biochimica et biophysica acta.

[33]  David Andreu,et al.  Ranacyclins, a new family of short cyclic antimicrobial peptides: biological function, mode of action, and parameters involved in target specificity. , 2003, Biochemistry.

[34]  M. Zasloff.  Antimicrobial peptides of multicellular organisms , 2002, Nature.

[35]  M. Aguilar,et al.  Measurement of the affinity of melittin for zwitterionic and anionic membranes using immobilized lipid biosensors. , 2001, The journal of peptide research : official journal of the American Peptide Society.

[36]  A. Plant,et al.  Phospholipid/alkanethiol bilayers for cell-surface receptor studies by surface plasmon resonance. , 1995, Analytical biochemistry.

[37]  B. Bechinger,et al.  The structure, dynamics and orientation of antimicrobial peptides in membranes by multidimensional solid-state NMR spectroscopy. , 1999, Biochimica et biophysica acta.

[38]  N. Fujii,et al.  An antimicrobial peptide, magainin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation. , 1996, Biochemistry.

[39]  M. Vaara,et al.  Agents that increase the permeability of the outer membrane. , 1992, Microbiological reviews.

[40]  A. Clayton,et al.  Kinetics of membrane lysis by custom lytic peptides and peptide orientations in membrane. , 2001, European journal of biochemistry.

[41]  Niv Papo,et al.  New lytic peptides based on the D,L-amphipathic helix motif preferentially kill tumor cells compared to normal cells. , 2003, Biochemistry.

[42]  N. Surolia,et al.  Surface Plasmon Resonance Studies Resolve the Enigmatic Endotoxin Neutralizing Activity of Polymyxin B* , 1999, The Journal of Biological Chemistry.

[43]  Y. Shai,et al.  Selective Cytotoxicity of Dermaseptin S3 toward IntraerythrocyticPlasmodium falciparum and the Underlying Molecular Basis* , 1997, The Journal of Biological Chemistry.