Article Detail

Home > Article Detail
  • P-ISSN 1225-0163
  • E-ISSN 2288-8985

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

Analytical Science and Technology / Analytical Science and Technology, (P)1225-0163; (E)2288-8985
2011, v.24 no.6, pp.460-466
https://doi.org/10.5806/AST.2011.24.6.460

  • Downloaded
  • Viewed

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


Reference

1

1. R. Latorre and O. Alvarez, Physiol. Rev., 61, 77-150 (1981).

2

2. H. Steiner, D. Hultmark, A. Engstrom, H. Bennich, H. G. Boman, Nature, 292, 246-248 (1981).

3

3. 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).

4

4. K. J. Hallock, D. K. Lee and A. Ramamoorthy, Biophys. J., 84, 3052-3060 (2003).

5

5. P. M Hwang and H. J. Vogel, Biochem. Cell Biol., 76, 235-246 (1998).

6

6. M. Zasloff, Proc. Natl. Acad. Sci. U.S.A., 84, 5449-5453 (1987).

7

7. J. J. Buffy, A. J. Waring and M. Hong, J. Am. Chem. Soc., 127, 4477-4483 (2005).

8

8. M. R. Yeaman and N. Y. Yount, Pharmacol. Rev., 55, 27-55 (2003).

9

9. R. Mani, A. J. Waring, R. I. Lehrer and M. Hong, Biochim. Biophys. Acta, Biomembr., 1716, 11-18 (2005).

10

10. 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).

11

11. O. Toke, Biopolymers, 80, 717-735 (2005).

12

12. A. Pokorny and P. F. F. Almeida, Biochemistry, 44, 9538-9544 (2005).

13

13. K. Matsuzaki, O. Murase, N. Fujii and K. Miyajima, Biochemistry, 34, 6521-6526 (1995).

14

14. K. Matsuzaki, K.-I. Sugishita, N. Ishibe, M. Ueha, S. Nakata, K. Miyajima and R. M. Epand, Biochemistry 37, 11856-11863 (1998).

15

15. Y. Herasimenka, M. Benincasa, M. Mattiuzzo, P. Cescutti, R. Gennaro and R. Rizzo, Peptides, 26, 1127-1132 (2005).

16

16. J.-A. Richard, I. Kelly, D. Marion, M. Pezolet and M. Auger, Biophys. J., 83, 2074-2083 (2002).

17

17. S. Yamaguchi, T. Hong, A. Waring, R. I. Lehrer, M. Hong, Biochemistry, 41, 9852-9862 (2002).

18

18. B. Bechinger, Biochim. Biophys. Acta, Biomembr., 1712, 101-108 (2005).

19

19. R. Mani, M. Tang, X. Wu, J. J. Buffy, A. J. Waring, M. A. Sherman and M. Hong, Biochemistry, 45, 8341-8349 (2006).

20

20. J. J. Buffy, M. J. McCormick, S. Wi, A. Waring, R. I. Lehrer and M. Hong, Biochemistry, 43, 9800-9812 (2004).

21

21. S. Wi and C. Kim, J. Phys. Chem. B, 112, 11402-11414 (2008).

22

22. C. Kim and S. Wi, Bull. Korean Chem. Soc., in press, (2012).

23

23. K. Matsuzaki, O. Murase and K. Miyajima, Biochemistry, 34, 12553-12559 (1995).

24

24. S. J. Ludtke, K. He, Y. Wu and H. W. Huang, Biochim. Biophys. Acta, Biomembr., 1190, 181-184 (1994).

25

25. R. Mani, J. J. Buffy, A. J. Waring, R. I. Lehrer and M. Hong, Biochemistry, 43, 13839-13848 (2004).

26

26. K. J. Hallock, D.-K. Lee, J. Omnaas, H. I. Mosberg and A. Ramamoorthy, Biophys. J., 83, 1004-1013(2002).

27

27. E. W. Washburn, C. J. West and C. Hull, International Critical Tables of Numerical Data, Physics, Chemistry, and Technology; McGraw-Hill: New York, 1926.

  • Downloaded
  • Viewed
  • 0KCI Citations
  • 0WOS Citations

Other articles from this issue

Recommanded Articles

상단으로 이동

Analytical Science and Technology