ライフサイエンスコーパス: magainin

1 ntimicrobial peptides found in nature (e.g., magainins).

2 or neutral porphyrin, to a CAMP, buforin or magainin.

3 coli after conjugation to either buforin or magainin.

4 one to graded in the mutants of cecropin and magainin.

5 ic than other antimicrobial peptides such as magainin.

6 Unlike magainin 1 and cecropin P1, alpha-helical antimicrobial

7 he human defensin HNP-1 and the frog peptide magainin 1 elicited export of 17-kDa IL-1beta, but these

8 ement of birefringence during the binding of magainin 2 (Mag2) and a highly potent analogue in which

9 Magainin 2 (MAG2) and PGLa are two alpha-helical antimic

10 PGLa and magainin 2 (MAG2) are amphiphilic antimicrobial peptides

11 Magainin 2 (S8A, G13A, G18A) is a designed variant that

12 The crystal structure of magainin 2 (S8A, G13A, G18A), obtained for the racemic f

13 f two prototypical linear cationic peptides: magainin 2 amide (which is selective for bacterial cells

14 ties than the natural antimicrobial peptides magainin 2 amide and cecropin B amide.

15 Ala19-magainin 2 amide exhibits both alpha-helix and beta-shee

16 xperiments indicate that alpha-helical Ala19-magainin 2 amide is bound near the phospholipid head gro

17 results obtained with two well-studied AMPs, magainin 2 and mastoparan X, and two model membranes ind

18 ance to protamine and alpha-helical peptides magainin 2 and melittin but not to beta-sheet defensin H

19 Magainin 2 and PGLa are among the best-studied cationic

20 While both magainin 2 and pleurocidin are capable of disrupting bac

21 of which rendered Salmonella susceptible to magainin 2 and polymyxin B, but not defensin HNP-1.

22 The slyA mutant was hypersensitive to magainin 2 and polymyxin B, suggesting that the virulenc

23 for resistance to the antimicrobial peptides magainin 2 and polymyxin B.

24 play a role in the antibacterial activity of magainin 2 and related peptides.

25 hoP regulated and required for resistance to magainin 2 but not to polymyxin B or defensin HNP-1.

26 mate crystals that contain the d form of the magainin 2 derivative along with an l-peptide in which o

27 usly reported racemic crystal structure of a magainin 2 derivative displayed a homochiral antiparalle

28 e-active antibacterial peptide cecropin A or magainin 2 failed to inhibit the DnaK-mediated phosphate

29 Host-defense peptides (HDPs) such as magainin 2 have emerged as potential therapeutic agents

30 in-plane scattering detects pores formed by magainin 2 in membranes only when a substantial fraction

31 ary structure and location of an analogue of magainin 2 in synthetic phospholipid bilayers using a co

32 We conclude that IAPP and magainin 2 induce membrane leakage and cytotoxicity thro

33 membranes by antimicrobial peptides such as magainin 2 is a significant activity performed by innate

34 Thus, magainin 2 is more sensitive to anionic lipid content th

35 The antiparallel dimer structure in the magainin 2 simulations resembles previously determined N

36 Remarkably, we observe IAPP and magainin 2 to be fully cross-cooperative in the inductio

37 nd insertion from solution of pleurocidin or magainin 2 to membranes representing the inner membrane

38 and helical tilt of an antimicrobial peptide magainin 2 using aligned X-band spin-label EPR spectrosc

39 anti-inflammatory effects of cecropin A(1-8)-magainin 2(1-12) hybrid peptide analog P5 on M. furfur.

40 ed for resistance to polymxyin B (but not to magainin 2) and is post-transcriptionally activated by t

41 D-Pyrrhocoricin, magainin 2, or buforin II, an antimicrobial peptide invo

42 onformational flexibility when compared with magainin 2, resists self-association at the membrane sur

43 crobial peptides including the alpha-helical magainin 2, the beta-sheet defensins and the cyclic lipo

44 tivity was found for the concerted action of magainin 2, the fungicidal lipopeptide class of surfacti

45 e antimicrobial peptide MSI-99, an analog of magainin 2, was expressed via the chloroplast genome to

46 e of the widely studied host-defense peptide magainin 2.

47 he sequences of delta-lysin, cecropin A, and magainin 2.

48 robial peptide cecropin A is tested here for magainin 2.

49 A cysteine substitution analogue of magainin-2 amide (magainin-F12W, N22C; denoted here as m

50 l peptides, MSI-78 and MSI-594, derived from magainin-2 and melittin, is presented.

51 Magainin, a 23-residue antibiotic peptide, interacts dir

52 Since magainin activity is modulated by oligomerization within

53 d that the helical peptides, alamethicin and magainin, also exhibit two distinct OCD basis spectra-on

54 Using the magainin analogue, pexiganan, as a model peptide we show

55 ries was essentially null, while fluorinated magainin analogues displayed an increase in hemolysis co

56 or oligomerization of specific highly active magainin analogues in membrane mimetic systems, we studi

57 ane-active antimicrobial peptides, including magainin and cecropin.

58 r to helical antimicrobial peptides, such as magainin and melittin.

59 istent with the two-state model exhibited by magainin and other small pore-forming peptides.

60 o two representative antimicrobial peptides, magainin and protegrin.

61 the toroidal pore model, first proposed for magainin and subsequently applied to PG-1.

62 t members of the alpha- and theta-defensins, magainins and cathelicidins had substantially higher lei

63 on of natural antimicrobial peptides such as magainins and cecropins.

64 Neutron diffraction shows that magainins and protegrins form stable pores in fully hydr

65 alpha- and -defensin-, magainin-, and cathelicidin-type antimicrobial peptides

66 the diffraction patterns of alamethicin and magainin are similar to gramicidin except in the scale o

67 Magainins are antimicrobial peptides that selectively di

68 Magainins are cationic, membrane-active peptides which s

69 elittin pores are closely similar to that of magainin but unlike that of alamethicin.

70 anism, no peptide oligomerization occurs and magainin catalyzes dye release in proportion to its conc

71 nfiguration is consistent with all published magainin data.

72 ith antibiotic activity similar to that of a magainin derivative against four bacterial species, incl

73 defense antimicrobial peptides, buforin and magainin, display moderately better protease stability w

74 that are lysed or porous, demonstrating that magainin disruption is a highly stochastic process.

75 e substitution analogue of magainin-2 amide (magainin-F12W, N22C; denoted here as mag-N22C), and a di

76 PGLa, a 21-residue member of the magainin family of antibiotic peptides, is shown to be h

77 n as a synthetic analog to peptides from the magainin family.

78 But overall, magainin follows the same all-or-none kinetic model as c

79 clearly indicating that both alamethicin and magainin form pores in membranes but of different sizes.

80 Magainin, found in the skin of Xenopus laevis, belongs t

81 the role of self-association in determining magainin function.

82 rall goal of this study was to apply the AMP magainin I as a recognition element for Escherichia coli

83 ere used to demonstrate that the immobilized magainin I can bind Salmonella with detection limits sim

84 We immobilized magainin I on silanized glass slides using biotin-avidin

85 The semiselective antimicrobial peptide magainin I--which occurs naturally on the skin of Africa

86 f the wild type (wt) to other CAMPs, such as Magainin II amide, hNP1-3, LL-37, and lactoferrin.

87 e membrane anchored by antimicrobial peptide magainin II and a phosphatidylethanolamine lipid derivat

88 pticin, indolicidin, puroindoline A peptide, magainin II F5W, lactoferrampin B, MIP3alpha51-70, and h

89 Melittin and magainin II were the most reactive peptides, with signif

90 The peptides examined include melittin, magainin II, PGLa, LAK1, LAK3 and penetratin.

91 : lysine for melittin; serine and lysine for magainin II.

92 , antibiotics, and the antimicrobial peptide magainin, indicating that the degP phenotype was not lim

93 Data from alamethicin- and magainin-induced pores are presented.

94 We demonstrate that magainin-induced pores in lipid vesicles have a mean dia

95 ectron microscopy, we have directly observed magainin interacting with synthetic DMPC/DMPG membranes.

96 Other peptides, including magainins, melittin and protegrins, all appear to induce

97 Magainin monomers play the role of fillers in the expans

98 id interactions of two synthetic variants of magainins (MSI-78 and MSI-594) originally designed by Ge

99 nted circular dichroism has detected helical magainin oriented perpendicular to the plane of the memb

100 The effect is most prominent in magainin patterns, which are used to demonstrate the met

101 Magainin pores exhibit intermembrane correlations.

102 distinct bound states in lipid bilayers like magainins, protegrins, alamethicin, and melittin that we

103 duced it into a phoP mutant and selected for magainin-resistant clones.

104 Conjugation to magainin resulted in the considerable strengthening of t

105 When magainin samples were further dehydrated or cooled, the

106 ated analogues in the buforin and two in the magainin series were prepared and analyzed for (1) their

107 ve molecules, including pore-forming peptide magainin, the turmeric (curry) extract curcumin, and det

108 Direct attachment of magainin to the substrate surface not only decreased non

109 s accelerated when the antimicrobial peptide magainin was used to anchor trivalent recognition, or wh

110 milies such as cathelicidins, cecropins, and magainins we demonstrate that designed antagonists can c

111 amethicin and that to the toroidal model for magainin were reviewed.