Phospholipids antimicrobial peptide

Papo N, Shai Y (2003) Can we predict biological activity of antimicrobial peptides from their interactions with model phospholipid membranes Peptides 24 1693-1703... 

Matsuzaki K, Murase O, Fujii N, Miyajima K (1996) An antimicrobial peptide, magainin 2, induced rapid flip-flop of phospholipids coupled with pore formation and peptide translocation. Biochemistry-Us 35 11361-11368... 

Other peptides containing histidines listed in Table 16.2, such as those of the histatin family (antimicrobial peptides), Sea Urchin (B18) and LAH4, strongly interact with phospholipid membranes and destabilize them. LAH4, which does not contain other cationic residues, exhibits a-helix and is more active in an acidic medium. These peptides could be putative endosome disrupting helpers that have not yet been used for polyfection. 

Prenner EJ, Lewis RNAH, McElhaney RN. The interaction of the antimicrobial peptide gramicidin S with lipid bilayer model and biological membranes. Biochim. Biophys. Acta 1999 1462 201-221. Papahadjonponlos D, Moscarello M, Eylar EH, Isaac T. Effects of proteins on thermotropic phase transitions of phospholipid membranes. Biochim. Biophys. Acta 1975 401 317-335. 

Kanithasen, N. (2005) 2H- and ViF-solid-stale NMR studies of the antimicrobial peptide (KIAGKIAf in phospholipid bilayers, Diploma thesis, University of Karlsruhe. 

Antimicrobial peptides, isolated from the dorsal glands of Australian tree frogs, have been studied using multinuclear solid state NMR. Specifically N-labelled peptides were studied using solid state NMR to determine their structure and orientation in model lipid bilayers. The effect of these peptides on phospholipid membranes was determined by and P solid state NMR... 

Much data have now shown that peptides, proteins, and lipids exhibit antimicrobial activity. The selective toxicity of peptides toward bacterial cells is primarily due to an initial electrostatic interaction between the peptide and the anionic phospholipid headgroups in the outer leaflet of the bacterial cytoplasmic membrane (Zasloff, 1987 Yeaman and Yount, 2003). A diversity of antimicrobial peptide sequences and structures have been discovered (Yeaman and Yount, 2003 Lai and GaUo, 2009), and this diversity underscores the reality that no single antimicrobial peptide sequence has emerged as an effective antimicrobial. Furthermore, the diversity of molecules as antimicrobials may be an evolutionary strategy to prevent or delay the development of microbial resistance to antimicrobial peptides. 

Antimicrobial peptides have been investigated by solid-state NMR spectroscopy when they are reconstituted into oriented phospholipid bilayers. Solid-state NMR spectroscopy have shown that magainins exhibit potent antimicrobial activities when their cationic amphipathic helix is oriented parallel to the bilayer surface, a configuration found in later years for many other linear cationic amphipathic peptides. This was different for other classes of peptides. In addition the effect on the membrane was also examined by P and NMR. 

Hansen et al. showed from molecular dynamics experiments P NMR solid state spectra are simulated. This was used to investigate the interaction between of lipid bilayers containing the antimicrobial peptides e.g. alamethicin. Close agreement was found for a range of peptides between simulation and experimental results. A comment was made on the diffusion rate of the phospholipids and the effect it has the NMR spectra. ... 

Ningsih, Z. Hossain, M. A. Wade, J. D. Clayton, A. H. A. Gee, M. L. Slow insertion kinetics during interaction of a model antimicrobial peptide with unilamellar phospholipid vesicles. Langmuir 2012, 28, 2217-2224. 

Shai Y (1999) Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by a-helical antimicrobial and cell non-selective membrane-lytic peptides. Biochim Biophys Acta 1462 55-70... 

The interactions of several peptides with phospholipids have been studied by computer simulation. Emphasis has been given to several aspects of protein-phospholipid interactions, including the way of association and orientational preference of peptides in contact with a bilayer, the effect of phospholipids on the preference and stability of helical conformations, and the effect of the inserted peptide on the structure and dynamics of the phospholipids. These investigations have been extended to bundles of helices and even whole pore-forming proteins. In particular, the simulation of ion channels and of peptides with antimicrobial action has attracted a great deal of attention in theoretical studies. 

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