Browse > Article
http://dx.doi.org/10.5806/AST.2011.24.6.460

A solid-state NMR study on the activity of an antimicrobial peptide, magainin 2  

Kim, Chul (Department of Chemistry, Hannam University)
Publication Information
Analytical Science and Technology / v.24, no.6, 2011 , pp. 460-466 More about this Journal
Abstract
The activity of an antimicrobial peptide, magainin 2, on lipid membranes was investigated using solid-state NMR and a new sampling method that employed mechanically aligned bilayers between thin glass plates. The experiments were performed at two hydration levels. At 95% hydration about 15% of the lipid bilayers were disrupted and at full hydration 20% were disrupted. From the comparison of two equilibrium states established by two sampling methods the importance of peptide binding to the lipid bilayer for whole membrane disruption was demonstrated.
Keywords
antimicrobial peptide; lipid bilayer; hydration; solid-state NMR;
Citations & Related Records
Times Cited By KSCI : 1  (Citation Analysis)
연도 인용수 순위
1 K. Matsuzaki, K.-I. Sugishita, N. Ishibe, M. Ueha, S. Nakata, K. Miyajima and R. M. Epand, Biochemistry 37, 11856-11863 (1998).   DOI   ScienceOn
2 Y. Herasimenka, M. Benincasa, M. Mattiuzzo, P. Cescutti, R. Gennaro and R. Rizzo, Peptides, 26, 1127-1132 (2005).   DOI   ScienceOn
3 J.-A. Richard, I. Kelly, D. Marion, M. Pezolet and M. Auger, Biophys. J., 83, 2074-2083 (2002).   DOI   ScienceOn
4 S. Yamaguchi, T. Hong, A. Waring, R. I. Lehrer, M. Hong, Biochemistry, 41, 9852-9862 (2002).   DOI   ScienceOn
5 B. Bechinger, Biochim. Biophys. Acta, Biomembr., 1712, 101-108 (2005).   DOI   ScienceOn
6 R. Mani, M. Tang, X. Wu, J. J. Buffy, A. J. Waring, M. A. Sherman and M. Hong, Biochemistry, 45, 8341-8349 (2006).   DOI   ScienceOn
7 J. J. Buffy, M. J. McCormick, S. Wi, A. Waring, R. I. Lehrer and M. Hong, Biochemistry, 43, 9800-9812 (2004).   DOI   ScienceOn
8 S. Wi and C. Kim, J. Phys. Chem. B, 112, 11402- 11414 (2008).   DOI   ScienceOn
9 C. Kim and S. Wi, Bull. Korean Chem. Soc., in press, (2012).
10 K. Matsuzaki, O. Murase and K. Miyajima, Biochemistry, 34, 12553-12559 (1995).   DOI   ScienceOn
11 S. J. Ludtke, K. He, Y. Wu and H. W. Huang, Biochim. Biophys. Acta, Biomembr., 1190, 181-184 (1994)   DOI   ScienceOn
12 R. Mani, J. J. Buffy, A. J. Waring, R. I. Lehrer and M. Hong, Biochemistry, 43, 13839-13848 (2004).   DOI   ScienceOn
13 K. J. Hallock, D.-K. Lee, J. Omnaas, H. I. Mosberg and A. Ramamoorthy, Biophys. J., 83, 1004-1013 (2002).   DOI   ScienceOn
14 E. W. Washburn, C. J. West and C. Hull, International Critical Tables of Numerical Data, Physics, Chemistry, and Technology; McGraw-Hill: New York, 1926.
15 R. Latorre and O. Alvarez, Physiol. Rev., 61, 77-150 (1981).   DOI
16 P. M Hwang and H. J. Vogel, Biochem. Cell Biol., 76, 235-246 (1998).   DOI   ScienceOn
17 H. Steiner, D. Hultmark, A. Engstrom, H. Bennich, H. G. Boman, Nature, 292, 246-248 (1981).   DOI   ScienceOn
18 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, 9159-9162 (1989).   DOI   ScienceOn
19 K. J. Hallock, D. K. Lee and A. Ramamoorthy, Biophys. J., 84, 3052-3060 (2003).   DOI   ScienceOn
20 M. Zasloff, Proc. Natl. Acad. Sci. U.S.A., 84, 5449- 5453 (1987).   DOI   ScienceOn
21 J. J. Buffy, A. J. Waring and M. Hong, J. Am. Chem. Soc., 127, 4477-4483 (2005).   DOI   ScienceOn
22 M. R. Yeaman and N. Y. Yount, Pharmacol. Rev., 55, 27-55 (2003).   DOI   ScienceOn
23 R. Mani, A. J. Waring, R. I. Lehrer and M. Hong, Biochim. Biophys. Acta, Biomembr., 1716, 11-18 (2005).   DOI   ScienceOn
24 Y. Bai, S. Liu, P. Jiang, L. Zhou, J. Li, C. Tang, C. Verma, Y. Mu, R. W. Beuerman and K. Pervushin, Biochemistry, 48, 7229-7239 (2009).   DOI   ScienceOn
25 O. Toke, Biopolymers, 80, 717-735 (2005).   DOI   ScienceOn
26 A. Pokorny and P. F. F. Almeida, Biochemistry, 44, 9538-9544 (2005).   DOI   ScienceOn
27 K. Matsuzaki, O. Murase, N. Fujii and K. Miyajima, Biochemistry, 34, 6521-6526 (1995).   DOI   ScienceOn