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Antimicrobial peptide

Many organisms, from invertebrates to humans, rely on conserved cationic amphipathic oligopeptide sequences to augment the immune system [105]. These antimicrobial peptides (AMPs) are secreted by immune cells to serve as first-line, broad-spectrum antibiotics [105]. Cationic AMPs associate with negatively charged bacterial membranes. [Pg.179]


Zasloff, M. Magainins, a class of antimicrobial peptides from Xenopus skin Isolation, characterization of two active forms, and partial cDNA sequence of a precursor. Proc. Nad. Acad. Sci. USA 1987, 84, 5449-5453. [Pg.30]

Notwithstanding the aforementioned difficulty in detecting specific target proteins other than the types normally observed in the taxonomic fingerprints from whole bacteria MALDI spectra (i.e., ribosomal proteins), some other target proteins and protein-like materials have been studied directly from whole cells. For example, Lantibiotics, antimicrobial peptides secreted by Gram-positive bacteria have been detected directly from whole bacteria by MALDI-TOF MS.51 The lantibiotics nisin and lacticin 481 were detected from whole cells and crude supernatants. Surprisingly, better results were reported from whole cells than the supernatants. In this study the presence of variants... [Pg.142]

Li P, Chan HC, He B et al. An antimicrobial peptide gene found in the male reproductive system of rats. Science 2001 291(5509] 1783—1785. [Pg.33]

Keywords Solid-state NMR structure analysis 19F-labeling Membrane-active peptides Native biomembranes Oriented membrane models Antimicrobial peptides... [Pg.90]

Fig. 6 Illustration of representative cell envelopes from prokaryotes and eukaryotes that are typically encountered by antimicrobial peptides. The key components of the biomembranes and cell wall or giycocaiyx are shown, and the averaged protein content and typical dimensions are drawn to scale... Fig. 6 Illustration of representative cell envelopes from prokaryotes and eukaryotes that are typically encountered by antimicrobial peptides. The key components of the biomembranes and cell wall or giycocaiyx are shown, and the averaged protein content and typical dimensions are drawn to scale...
Unlike other Eukarya, animal cells lack cell walls, though they tend to be surrounded by a highly developed glycocalyx of up to 140 nm in thickness [108]. This diffuse layer of densely packed oligosaccharides has a heterogeneous composition and is connected to the membrane via lipids or integral proteins. The boundary of the cell usually extends beyond the mere lipid bilayer with its embedded proteins, and the extracellular structures provide initial sites of interaction or are themselves targets for MAPs such as antimicrobial peptides [115]. [Pg.104]

In summary, we may thus conclude that PGLa and GS do not form stable, NMR-observable pores in native membrane as readily as they do in model bilayers. The corresponding tilted and/or inserted states of our two representative MAPs could only be comprehensively characterized in DMPC-based samples, where the peptides could be trapped in a uniform state. In living cells, on the other hand, these states would seem to be only of a transient nature, i.e. at the very moment when the antimicrobial peptide attacks the membrane and passes through the lipid barrier along its concentration gradient towards the cytosol. [Pg.107]

Ramamoorthy A (2009) Beyond NMR spectra of antimicrobial peptides dynamical images at atomic resolution and functional insights. Solid State Nucl Mag 35 201-207... [Pg.112]

Zelezetsky I, Tossi A (2006) Alpha-helical antimicrobial peptides - using a sequence template to guide structure-activity relationship studies. BBA-Biomembranes 1758 1436-1449... [Pg.112]

Scott RW, DeGrado WF, Tew GN (2008) De novo designed synthetic mimics of antimicrobial peptides. Curr Opin Biotechnol 19 620-627... [Pg.113]

Epand RM, Vogel FIJ (1999) Diversity of antimicrobial peptides and their mechanisms of action. BBA-Biomembranes 1462 11-28... [Pg.113]

Giuliani A, Pirri G, Bozzi A, Di Giulio A, Aschi M, Rinaldi AC (2008) Antimicrobial peptides natural templates for synthetic membrane-active compounds. Cell Mol Life Sci 65 2450-2460... [Pg.113]

Glaser RW, Sachse C, Durr UHN, Wadhwani P, Ulrich AS (2004) Orientation of the antimicrobial peptide PGLa in lipid membranes determined from F-19-NMR dipolar couplings of 4-CF3-phenylglycine labels. J Magn Reson 168 153-163... [Pg.113]

Strandberg E, Ulrich AS (2004) NMR methods for studying membrane-active antimicrobial peptides. Concepts Magn Reson A 23A 89-120... [Pg.114]

Aisenbrey C, Bertani P, Bechinger B (2010) Solid-state NMR investigations of membrane-associated antimicrobial peptides. Methods Mol Biol 618 209-233... [Pg.114]

Tremouilhac P, Strandberg E, Wadhwani P, Ulrich AS (2006) Conditions affecting the realignment of the antimicrobial peptide PGLa in membranes as monitored by solid state H-2-NMR. BBA-Biomembranes 1758 1330-1342... [Pg.116]

Afonin S, Durr UHN, Wadhwani P, Salgado J, Ulrich AS (2008) Solid state NMR structure analysis of the antimicrobial peptide gramicidin S in lipid membranes concentration-depen-dent re-alignment and self-assembly as a beta-barrel. Top Curr Chem 273 139-154... [Pg.116]

Kosol S, Zangger K (2010) Dynamics and orientation of a cationic antimicrobial peptide in two membrane-mimetic systems. J Struct Biol 170 172-179... [Pg.116]

Yeaman MR, Yount NY (2003) Mechanisms of antimicrobial peptide action and resistance. [Pg.116]

Papo N, Shai Y (2003) Can we predict biological activity of antimicrobial peptides from their interactions with model phospholipid membranes Peptides 24 1693-1703... [Pg.117]

Ruden S, Hilpert K, Berditsch M, Wadhwani P, Ulrich AS (2009) Synergistic interaction between silver nanoparticles and membrane-permeabilizing antimicrobial peptides. Antimicrob Agents Chemother 53 3538-3540... [Pg.117]

Mangoni ML, Rinaldi AC, Di Giulio A, Mignogna G, Bozzi A, Barra D, Simmaco M (2000) Structure-function relationships of temporins, small antimicrobial peptides from amphibian skin. Eur J Biochem 267 1447-1454... [Pg.118]

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... [Pg.118]

Blazyk J, Wiegand R, Klein J, Hammer J, Epand RM, Epand RF, Maloy WL, Kari UP (2001) A novel linear amphipathic beta-sheet cationic antimicrobial peptide with enhanced selectivity for bacterial lipids. J Biol Chem 276 27899-27906... [Pg.118]

Antimicrobial peptide MSI-99 tml/tmA Prrn ggagg/TpsbA 21.5-47% Daniell... [Pg.117]

Beisswenger, C. and Bals, R., Antimicrobial peptides in lung inflammation, Chem. Immunol. Allergy. 86, 55, 2005. [Pg.321]

PO = phenoloxidase, AMPs = antimicrobial peptides, NK cells = natural killer cells. Adapted from Flajnik and Du... [Pg.369]


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Antimicrobial activity peptides

Antimicrobial peptides (AMP

Antimicrobial peptides LEAPS

Antimicrobial peptides QSAR studies

Antimicrobial peptides aquaculture

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Antimicrobial peptides circulation

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Antimicrobial peptides magainin

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