ライフサイエンスコーパス: alamethicin

1 nella antibody and the antimicrobial peptide alamethicin.

2 -4 A deeper into the membrane than is native alamethicin.

3 ty and the voltage-gated channel activity of alamethicin.

4 ays that are inducible by a fungal elicitor, alamethicin.

5 ty of naturally occurring peptaibols such as alamethicin.

6 milar to that of magainin but unlike that of alamethicin.

7 e concentration-gated mechanism of action as alamethicin.

8 he backbone of the exposed C-terminal end of alamethicin.

9 -4 A deeper in the membrane than does native alamethicin.

10 least 1000 times faster than that of native alamethicin.

11 part of the high-order structure of inserted alamethicin.

12 rallel transmembrane arrays of reconstituted alamethicin.

13 me of water [D2O:dioleoylphosphatidylcholine:alamethicin; 220:1:0.05; (M:M:M)], the exchange-protecti

14 to record the smallest conductance state of alamethicin (24 pS) at an unprecedentedly high bandwidth

15 th fluorescence detection of NADH and use of alamethicin, a channel-forming antibiotic that enables a

16 g access for NADH to intact mitochondria via alamethicin, a channel-forming antibiotic.

17 ast mitochondrial unspecific channel, and to alamethicin, a membrane-disrupting agent.

18 The aqueous-membrane partitioning of alamethicin, a voltage-gated channel-forming peptide, wa

19 Alamethicin, a voltage-gated peptide channel for which m

20 d BLMs that retain the fluidity required for alamethicin activity yet are stable for several days as

21 indicate that, under the conditions studied, alamethicin adopts a stable helical structure in DOPC bi

22 us x-ray diffraction measurement showed that alamethicin adsorbed on the surface has the effect of th

23 Alamethicin adsorbs on the membrane surface at low pepti

24 sent direct visualization of pores formed by alamethicin (Alm) in a matrix of phospholipids using ele

25 ics simulation of the archetype barrel-stave alamethicin (alm) pore in a 1,2-dioleoyl-sn-glycero-3-ph

26 ating the ion channels Gramicidin A (gA) and Alamethicin (ALM).

27 Alamethicins (ALMs) are antimicrobial peptides of fungal

28 increased in the presence of Triton X-100 or alamethicin, an ionophore that facilitates movement of U

29 reases the permeability of the membranes, or alamethicin, an ionophore that facilitates transmembrane

30 The alamethicin analog L1 exhibits crossing rates that are a

31 gration rate of the C-terminal end of native alamethicin and a more hydrophobic analog called L1.

32 Studies employing alamethicin and inhibitors were able to again localize t

33 full hydration, the diffraction patterns of alamethicin and magainin are similar to gramicidin excep

34 of scattering), clearly indicating that both alamethicin and magainin form pores in membranes but of

35 eviously reported that the helical peptides, alamethicin and magainin, also exhibit two distinct OCD

36 er normal growth but is induced in leaves by alamethicin and methyl jasmonate treatments.

37 channel electrical recordings of the peptide alamethicin and of the proteoliposome-delivered potassiu

38 dence that led to the barrel-stave model for alamethicin and that to the toroidal model for magainin

39 e is assayed in the presence of 40 microg/ml alamethicin and the reaction is terminated by H(2)SO(4),

40 nstants for amides in membrane-reconstituted alamethicin and those for amides in alamethicin dissolve

41 dynamic ion channels (gramicidin A (gA) and alamethicin) and one static biological nanopore (alpha-h

42 n lipid bilayers like magainins, protegrins, alamethicin, and melittin that were previously studied.

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

44 Thus, the G-X-X-P motif found in alamethicin appears to be largely responsible for mediat

45 ll the potentially hydrogen-bonded amides of alamethicin are at least 1000-fold exchange protected in

46 d that barrel-stave-forming peptides such as alamethicin are not line-active, and that the seemingly

47 ivity that is seen in the binding curves for alamethicin are postulated to be a result of a localized

48 In vesicles containing alamethicin at molar ratios between 1:20 and 1:100 relat

49 When the free-energy changes for alamethicin binding are compared with the previously det

50 ttern is reproducible by melittin, LL37, and alamethicin but not by CCCP or daptomycin, agents known

51 pmol of the pore-forming, antibiotic peptide alamethicin can be detected visually with this system.

52 It shows that the binding of a derivative of alamethicin carrying a covalently attached sulfonamide l

53 Our results suggest that the alamethicin channel in a lipid bilayer is a good model s

54 allows the introduction of species, such as alamethicin channels, into preformed lipid bilayers via

55 f Keller et al. regarding the conductance of alamethicin channels.

56 ced peptides that we have investigated, only alamethicin conforms to the barrel-stave model.

57 The slow rate of alamethicin crossing can be explained if the peptide hel

58 res of DOPC/DOPE is increased the binding of alamethicin decreases, and the increase in binding free

59 oration of the voltage-dependent pore-former alamethicin did slightly reduce lipid lateral mobility.

60 stituted alamethicin and those for amides in alamethicin dissolved directly into D2O buffer.

61 In this configuration alamethicin does not completely cross the bilayer, and t

62 Native alamethicin exhibits a very slow transmembrane migration

63 Some membrane peptides, such as Alamethicin, form barrel-stave aggregates with a broad p

64 Alamethicin forms pores in a narrow range of size.

65 The membrane position and structure of alamethicin found here limit the likely models for volta

66 scale two-dimensional crystalline domains of alamethicin helices, oriented parallel to the air/water

67 of the barrel-stave type consisting of eight alamethicin helices.

68 en observed in the central helical domain of alamethicin in methanol.

69 which differs from the barrel-stave model of alamethicin in that the lipid bends back on itself like

70 Alamethicin in the inserted state was prepared and undeu

71 transmembrane peptide pores gramicidin A and alamethicin in the lipid bilayer they can achieve ionic

72 structed the electron density profile of the alamethicin-induced transmembrane pore by x-ray diffract

73 on energy is the major driving force for the alamethicin insertion transition.

74 r concentrations P/L > or = 1/15, all of the alamethicin inserts into the membrane and forms well-def

75 When partitioning of alamethicin into the aqueous phase was suppressed by hyd

76 Alamethicin is a helical 20-amino acid voltage-gated cha

77 g" model of the voltage-gated ion channel of alamethicin is inferred from the structural results pres

78 The distances show that alamethicin is inserted along the bilayer normal with th

79 ge with D2O buffer in membrane-reconstituted alamethicin is interpreted in terms of stabilization by

80 Alamethicin is the archetypal antimicrobial pore-forming

81 ely cross the bilayer, and the N-terminus of alamethicin is within the membrane hydrocarbon approxima

82 ntial to achieve voltage-dependent gating or alamethicin-like behavior.

83 prepared fully hydrated multiple bilayers of alamethicin-lipid mixtures in a condition where pores we

84 d uncoupling, when uncoupling arises through alamethicin-mediated pore formation, or upon opening the

85 olecular dynamics simulation of the peptides alamethicin, melittin, cyclotide kalata B1, 18A, and KKp

86 in sharp contrast to the prevailing view of alamethicin oligomers formed by perfectly aligned helica

87 trates upon inner membrane pore formation by alamethicin or Ca(2+)-induced PTP opening.

88 er membrane pore formation induced by either alamethicin or calcium-induced PTP opening.

89 provide strong support for our finding that alamethicin peptides adopt a diverse set of configuratio

90 of peptide aggregation and pore formation by alamethicin peptides in a hydrated lipid bilayer.

91 ligomers formed by perfectly aligned helical alamethicin peptides in a lipid bilayer.

92 Evidence from alamethicin-permeabilized mitochondria suggests that TG

93 Furthermore, by using alamethicin-permeabilized mitochondria, we measured a si

94 es, the expression of AtBSMT1 was induced by alamethicin, Plutella xylostella herbivory, uprooting, p

95 The result unambiguously shows that the alamethicin pore is of the barrel-stave type consisting

96 odeled with the barrel-stave model after the alamethicin pore.

97 The pores are almost twice as large as the alamethicin pores.

98 by conformational differences between L1 and alamethicin rather than differences in hydrophobicity.

99 nstants were measured for backbone amides of alamethicin reconstituted in dioleoylphosphatidylcholine

100 ve studied voltage-dependent ion channels of alamethicin reconstituted into an artificial planar lipi

101 Alamethicin represents a hydrophobic alpha-helical pepti

102 ion to the peptide concentration, similar to alamethicin's membrane thinning effect.

103 ted] plants treated with the fungal elicitor alamethicin, showing that they are also formed in the in

104 the surface state and the insertion state of alamethicin, since they show a similar dependence on lip

105 ide, to the solution released CA II from the alamethicin-sulfonamide conjugate and restored the curre

106 imately 2 microM for the binding of CA II to alamethicin-sulfonamide in the bilayer recording chamber

107 direct structural methods to different lipid/alamethicin systems.

108 When compared to native alamethicin, the analog lacking proline 14 exhibited sim

109 substitutions alter the channel behavior of alamethicin, the macroscopic and single-channel currents

110 imal emission of MeSA was observed following alamethicin treatment of leaves.

111 The distances that are measured for alamethicin using EPR are consistent with a linear high

112 id ratios, which are the conditions at which alamethicin was tested for its antibacterial activity.

113 ne lipid unsaturation on the partitioning of alamethicin were also measured and are qualitatively con

114 led derivatives of the voltage-gated peptide alamethicin were prepared with nitroxides at the C-termi

115 he flexibility of this helix, two analogs of alamethicin were synthesized, one with proline 14 replac

116 ree spin-labeled derivatives of an analog of alamethicin where alpha-methylalanine residues are repla