The monolayer technique: a potent tool for studying the interfacial properties of antimicrobial and membrane-lytic peptides and their interactions with lipid membranes.
Erudites of the antiquity already knew the calming effect of oil films on the sea waves. But one had to wait until 1774 to read the first scientific report on oil films from B. Franklin and again 1878 to learn the thermodynamic analysis on adsorption developed by J. Gibbs. Then, in 1891, Agnes Pockels described a technique to manipulate oil films by using barriers. Finally, in 1917, I. Langmuir introduced the experimental and theoretical modern concepts on insoluble monolayers. Since that time, and because it has been found to provide invaluable information at the molecular scale, the monolayer technique has been more and more extensively used, and, during the past decade, an explosive increase in the number of publications has occurred. Over the same period, considerable and ever-increasing interest in the antimicrobial peptides of various plants, bacteria, insects, amphibians and mammals has grown. Because many of these antimicrobial peptides act at the cell membrane level, the monolayer technique is entirely suitable for studying their physicochemical and biological properties. This review describes monolayer experiments performed with some of these antimicrobial peptides, especially gramicidin A, melittin, cardiotoxins and defensin A. After giving a few basic notions of surface chemistry, the surface-active properties of these peptides and their behavior when they are arranged in monomolecular films are reported and discussed in relation to their tridimensional structure and their amphipathic character. The penetration of these antimicrobial peptides into phospholipid monolayer model membranes, as well as their interactions with lipids in mixed films, are also emphasized.
Maget-Dana
R
R
Centre de Biophysique Moléculaire, rue Charles Sadron, 45071, Orléans, France. maget@cnrs-orleans.fr
D000595:Amino Acid Sequence; D000818:Animals; D000900:Anti-Bacterial Agents / Q000737:chemistry*; D023181:Antimicrobial Cationic Peptides; D001426:Bacterial Proteins / Q000737:chemistry; D002462:Cell Membrane / Q000737:chemistry*; D023082:Defensins; D006096:Gramicidin / Q000737:chemistry; D006460:Hemolysin Proteins / Q000737:chemistry; D019476:Insect Proteins / Q000737:chemistry; D008051:Lipid Bilayers / Q000737:chemistry*; D008555:Melitten / Q000737:chemistry; D008563:Membrane Lipids / Q000737:chemistry; D008567:Membranes, Artificial; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009561:Nisin / Q000031:analogs & derivatives / Q000737:chemistry; D010455:Peptides / Q000737:chemistry*; D010743:Phospholipids / Q000737:chemistry; D011506:Proteins; D013499:Surface Properties
D000900:Anti-Bacterial Agents; D023181:Antimicrobial Cationic Peptides; D001426:Bacterial Proteins; D023082:Defensins; D006460:Hemolysin Proteins; D019476:Insect Proteins; D008051:Lipid Bilayers; D008563:Membrane Lipids; D008567:Membranes, Artificial; D010455:Peptides; D010743:Phospholipids; D011506:Proteins; C401901:androctonin protein, Androctonus australis; C044299:bombolitins; C058181:insect defensin A; D006096:Gramicidin; D009561:Nisin; D008555:Melitten; C025994:delta hemolysin protein, Staphylococcus aureus; C071364:nisin Z