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A 2H solid-state NMR study on the lipid phase change in the presence of an antimicrobial peptide
Analytical Science and Technology / Analytical Science and Technology, (P)1225-0163; (E)2288-8985
2013, v.26 no.1, pp.61-66
https://doi.org/10.5806/AST.2013.26.1.061
&
(2013). A 2H solid-state NMR study on the lipid phase change in the presence of an antimicrobial peptide. Analytical Science and Technology, 26(1), 61-66, https://doi.org/10.5806/AST.2013.26.1.061
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Abstract
The activity of an antimicrobial peptide, protegrin-1, on the well-aligned lipid bilayer deposited on a thin coverglass plate was investigated by 2H solid-state NMR spectroscopy. Orientational distribution and molecular motion in the lipid bilayer were determined from 2H solid-state NMR spectrum. Reorientational motion of lipid molecules in the vacuum-dried state was found to be small but their orientational distribution was not able to be determined. As storage times were longer, the order of the alignment of lipid molecules in the lipid bilayer and percentages involved in the toroidal pore structures increased. We found that much longer time is required to get the equilibrium state of the peptide-lipid mixture under our experimental condition for investigating the action of the antimicrobial peptide like protegrin-1 on the lipid bilayers deposited on the thin coverglass plates.
- keywords
- protegrin-1, antimicrobial peptide, lipid bilayer, solid-state NMR
Reference
1
H. Steiner, D. Hultmark, A. Engstrom, H. Bennich and H. G. Boman, Nature, 292(5820), 246-248 (1981).
2
J. Y. Lee, A. Boman, C. X. Sun, M. Andersson, H. Jornvall, V. Mutt and H. G. Boman, Proc. Natl. Acad. Sci. U. S. A., 86(23), 9159-9162 (1989).
3
R. Latorre and O. Alvarez, Physiol. Rev., 61(1), 77-150 (1981).
4
M. Zasloff, Proc. Natl. Acad. Sci. U. S. A., 84(15), 5449-5453 (1987).
5
P. M. Hwang and H. J. Vogel, Biochem. Cell Biol., 76(2/3), 235-246 (1998).
6
K. J. Hallock, D. K. Lee and A. Ramamoorthy, Biophys. J., 84(5), 3052-3060 (2003).
7
J. J. Buffy, A. J. Waring and M. Hong, J. Am. Chem. Soc., 127(12), 4477-4483 (2005).
8
M. R. Yeaman and N. Y. Yount, Pharmacol. Rev., 55(1), 27-55 (2003).
9
R. Mani, A. J. Waring, R. I. Lehrer and M. Hong, Biochim. Biophys. Acta, Biomembr., 1716(1), 11-18 (2005).
10
O. Toke, Biopolymers, 80(6), 717-735 (2005).
11
Y. Bai, S. Liu, P. Jiang, L. Zhou, J. Li, C. Tang, C. Verma, Y. Mu, R. W. Beuerman and K. Pervushin, Biochemistry, 48(30), 7229-7239 (2009).
12
A. Pokorny and P. F. F. Almeida, Biochemistry, 44(27), 9538-9544 (2005).
13
K. Matsuzaki, O. Murase, N. Fujii and K. Miyajima, Biochemistry, 34(19), 6521-6526 (1995).
14
K. Matsuzaki, K. Sugishita, N. Ishibe, M. Ueha, S. Nakata, K. Miyajima and R. M. Epand, Biochemistry, 37(34), 11856-11863 (1998).
15
J.-A. Richard, I. Kelly, D. Marion, M. Pezolet and M. Auger, Biophys. J., 83(4), 2074-2083 (2002).
16
Y. Herasimenka, M. Benincasa, M. Mattiuzzo, P. Cescutti, R. Gennaro and R. Rizzo, Peptides, 26(7), 1127- 1132 (2005).
17
V. N. Kokryakov, S. S. Harwig, E. A. Panyutich, A. A. Shevchenko, G. M. Aleshina, O. V. Shamova, H. A. Korneva and R. I. Lehrer, FEBS Lett., 327(2), 231-236 (1993).
18
R. L. Fahrner, T. Dieckmann, S. S. L. Harwig, R. I. Lehrer, D. Eisenberg and J. Feigon, Chem. Biol., 3(7), 543-550 (1996).
19
H. Jang, B. Ma and R. Nussinov, BMC Struct Biol, 7, 21 (2007).
20
L. Yang, T. M. Weiss, R. I. Lehrer and H. W. Huang, Biophys. J., 79(4), 2002-2009 (2000).
21
S. Yamaguchi, T. Hong, A. Waring, R. I. Lehrer and M. Hong, Biochemistry, 41(31), 9852-9862 (2002).
22
J. J. Buffy, A. J. Waring, R. I. Lehrer and M. Hong, Biochemistry, 42(46), 13725-13734 (2003).
23
J. J. Buffy, T. Hong, S. Yamaguchi, A. J. Waring, R. I. Lehrer and M. Hong, Biophys. J., 85(4), 2363-2373 (2003).
24
R. Mani, J. J. Buffy, A. J. Waring, R. I. Lehrer and M. Hong, Biochemistry, 43(43), 13839-13848 (2004).
25
C. Kim, J. Spano, E. K. Park and S. Wi, Biochim. Biophys. Acta, 1788(7), 1482-1496 (2009).
26
B. Bechinger, Biochim. Biophys. Acta, Biomembr., 1712(1), 101-108 (2005).
27
R. Mani, M. Tang, X. Wu, J. J. Buffy, A. J. Waring, M. A. Sherman and M. Hong, Biochemistry, 45(27), 8341- 8349 (2006).
28
J. J. Buffy, M. J. McCormick, S. Wi, A. Waring, R. I. Lehrer and M. Hong, Biochemistry, 43(30), 9800-9812 (2004).
29
S. Wi and C. Kim, J. Phys. Chem. B, 112(36), 11402- 11414 (2008).
30
K. J. L. Hallock, D.-K. and Ramamoorthy, A., Biophys. J., 84, 3052-3060 (2003).
31
J. Butterworth, Proceedings of the Physical Soc., 86, 297-304 (1965).
32
C. Kim, Bull. Korean Chem. Soc., 31(2), 372-378 (2010).
33
C. Kim, J. Korean Chem. Soc., 54(2), 183-191 (2010).
34
C. Kim, Anal. Sci. Technol., 24(6), 460-466 (2011).
35
L. S. Vermeer, B. L. de Groot, V. Reat, A. Milon and J. Czaplicki, Eur. Biophys. J., 36(8), 919-931 (2007).
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