Display Settings:

Items per page
We are sorry, but NCBI web applications do not support your browser and may not function properly. More information

Results: 10

1.
FIGURE 1

FIGURE 1. From: Membrane Insertion and Bilayer Perturbation by Antimicrobial Peptide CM15.

Structures of the MTSL and BrMTSL spin labels and the resulting side chains produced by reaction with the peptide cysteine residue.

Sara Pistolesi, et al. Biophys J. 2007 September 1;93(5):1651-1660.
2.
FIGURE 2

FIGURE 2. From: Membrane Insertion and Bilayer Perturbation by Antimicrobial Peptide CM15.

CD spectra of C4BrMTSL in 5 mM phosphate buffer (crosses) in 50% TFE (squares) and in the presence of LUVs at an L/P ratio of 100:1 (triangles). The peptide concentration was 0.1 mM (∼0.2 mg/ml) in each sample.

Sara Pistolesi, et al. Biophys J. 2007 September 1;93(5):1651-1660.
3.
FIGURE 3

FIGURE 3. From: Membrane Insertion and Bilayer Perturbation by Antimicrobial Peptide CM15.

EPR spectra of C4-MTSL in (A) 50 mM MOPS buffer, (B) in 50% TFE, and in the presence of PE/PG/CL (70:25:5) LUVs at L/P ratios of (C) 250:1, (D) 50:1, and (E) 25:1. Spectra for the membrane-bound peptide are presented at a 10-fold higher gain. The scan width is 100 G.

Sara Pistolesi, et al. Biophys J. 2007 September 1;93(5):1651-1660.
4.
FIGURE 10

FIGURE 10. From: Membrane Insertion and Bilayer Perturbation by Antimicrobial Peptide CM15.

Effect of wild-type CM15 binding on the EPR depth parameter. The depth parameter for 12PCSL (triangles), 7PCSL (circles), and 5PCSL (squares) is plotted against the L/P molar ratio. The spin labels were at a concentration of 1 mol % in PE/PG/CL LUVs. Error bars represent the standard deviation from at least three independent experiments.

Sara Pistolesi, et al. Biophys J. 2007 September 1;93(5):1651-1660.
5.
FIGURE 9

FIGURE 9. From: Membrane Insertion and Bilayer Perturbation by Antimicrobial Peptide CM15.

Effect of wild-type CM15 binding on the accessibility of PCSLs to NiEDDA. Large unilamellar liposomes (PE/PG/CL, molar ratio 70:25:5) containing 1 mol % of 5PCSL (squares), 7PCSL (circles), or 12PCSL (triangles) were mixed with CM15 to give the desired L/P ratio, incubated overnight at room temperature and the CW saturation parameter P1/2 determined under N2. Final NiEDDA concentration was 20 mM.

Sara Pistolesi, et al. Biophys J. 2007 September 1;93(5):1651-1660.
6.
FIGURE 6

FIGURE 6. From: Membrane Insertion and Bilayer Perturbation by Antimicrobial Peptide CM15.

Accessibilities of C4-MTSL (squares) and C4-BrMTSL (triangles) as a function of the L/P ratio. (A) The change in the EPR saturation parameter, P1/2, in the presence of 20 mM NiEDDA, (B) the change in P1/2 upon equilibration with air (20% O2), and (C) the EPR depth parameter, calculated as described in the text. Error bars indicate standard deviations from at least three separate measurements.

Sara Pistolesi, et al. Biophys J. 2007 September 1;93(5):1651-1660.
7.
FIGURE 5

FIGURE 5. From: Membrane Insertion and Bilayer Perturbation by Antimicrobial Peptide CM15.

EPR spectra of C4MTSL bound to membranes in the frozen state. C4MTSL was mixed with LUVs at final L/P ratios of (A) 160:1, (B) 80:1, (C) 40:1, and (D) 20:1 and allowed to equilibrate at room temperature for 1 h. The samples were then placed in the EPR cavity and brought to 200 K. Scan widths are 160 G. No changes in line widths or relative amplitudes were observed as a function of the L/P ratio.

Sara Pistolesi, et al. Biophys J. 2007 September 1;93(5):1651-1660.
8.
FIGURE 7

FIGURE 7. From: Membrane Insertion and Bilayer Perturbation by Antimicrobial Peptide CM15.

EPR spectra of (A) 5PCSL, (B) 7PCSL, and (C) 12PCSL in PE/PG/CL liposomes. In each set of spectra the upper spectrum is in the absence of peptide and the lower spectrum is in the presence of wild-type CM15 at an L/P ratio of 25:1. The increase in 2T// observed for 5- and 7PCSL indicate a decrease in rotational mobility. For 12PCSL there is no measurable difference in the width of the center line (ΔH0) or in the relative line amplitudes (A0 and A−1). Scan widths are 100 G for 5- and 7PCSL, and 80 G for 12PCSL.

Sara Pistolesi, et al. Biophys J. 2007 September 1;93(5):1651-1660.
9.
FIGURE 4

FIGURE 4. From: Membrane Insertion and Bilayer Perturbation by Antimicrobial Peptide CM15.

EPR spectra of C4-BrMTSL in (A) 50 mM MOPS buffer, (B) in 50% TFE, and in the presence of PE/PG/CL (70:25:5) LUVs at L/P ratios of (C) 250:1, (D) 50:1, and (E) 25:1. Scan width 100 G. Spectra for the membrane-bound peptide are presented at a 10-fold higher gain. Binding to the LUVs results in a pronounced reduction in spin label mobility, and the BrMTSL side chain is significantly more immobilized than the nonbrominated MTSL side chain in the membrane-bound state (compare with Fig. 3).

Sara Pistolesi, et al. Biophys J. 2007 September 1;93(5):1651-1660.
10.
FIGURE 8

FIGURE 8. From: Membrane Insertion and Bilayer Perturbation by Antimicrobial Peptide CM15.

Effect of wild-type CM15 binding on the motion of PCSLs. CM15 was added to PE/PG/CL (70:25:5) LUVs containing 1 mol % PCSL and equilibrated at room temperature overnight before recording the EPR spectrum. The motion parameter 2T// for 5PCSL (squares) and 7PCSL (triangles) is plotted as a function of the lipid ratio (with ∞ corresponding to control values in the absence of peptide). An increase in 2T// indicates decreased mobility of the spin label. Error bars indicate the standard deviation from at least three separate experiments.

Sara Pistolesi, et al. Biophys J. 2007 September 1;93(5):1651-1660.

Display Settings:

Items per page

Supplemental Content

Recent activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...
Write to the Help Desk