Biomaterials Research (생체재료학회지)

Korean Society for Biomaterials (한국생체재료학회)
권호 표지

An Effect of Resveratrol on the Formation of Lipid Membrane Fragmentations Caused by the Interaction Between Antimicrobial Peptide Pexiganan (MSI-78) and Lipid Bilayer Membranes

항균펩타이드인 Pexiganan (MSI-78) 과 모델 이중 지질막 간의 상호 작용으로 생성되는 지질막 파괴에서 Resveratrol 분자의 영향

  • You, Changsoo (Department of Fine Chemistry, Seoul National University of Science & Technology) ;
  • Jung, Junho (Department of Fine Chemistry, Seoul National University of Science & Technology) ;
  • Lee, Dongkuk (Department of Fine Chemistry, Seoul National University of Science & Technology)
  • 유창수 (서울과학기술대학교, 정밀화학과) ;
  • 정준호 (서울과학기술대학교, 정밀화학과) ;
  • 이동국 (서울과학기술대학교, 정밀화학과)
  • Received : 2013.10.25
  • Accepted : 2013.11.12
  • Published : 2013.12.01
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Abstract

This study has investigated the effect of Resveratrol(3,5,4'-trihydroxy-trans-stilbene) on membrane fragmentation of model lipid bilayer membranes caused by the antimicrobial peptide, Pexiganan (MSI-78). Large unilamellar vesicles (LUVs) of 7:3 POPC/POPG has been used for the model cellular membrane in the study of interaction between biomolecules and lipid molecules. Recently, this model was used to investigate lipid composition-dependent membrane fragmentation and pore-forming mechanism of membrane disruption by Pexigan (MSI-78). Results showed that the peptide induces micelle-like fragments evidenced by the $^{31}P$ NMR signal at 0 ppm compared to the typical powder pattern of unperturbed lipid bilayers. In the present study, Resveratrol molecules were added to the LUVs before the peptide was applied to them. $^{31}P$ spectra were collected for each sample and monitored any changes in the $^{31}P$ NMR spectra. Our observations show that resveratrol inhibits MSI-78 interaction to POPC/POPG lipid bilayer and protect the lipid membrane evidenced by the disappearance of the isotropic $^{31}P$ NMR intensity near 0.0 ppm. We suggest that resveratrol binds to the surface of the POPC/POPG bilayers and alters the properties of the lipid membrane.

Keywords

Acknowledgement

Supported by : National Research Foundation of Korea (NRF)

References

  1. Vanessa D, Christin K, Lindsay K, Mariya M, Wilson S, Carsten S, Duane F, Grant Z, Calmels F, Debruyne R, Golding GB, Poinar HN, Wright GD, "Antibiotic resistance is ancient," Nature, 477 (7365), 457-461 (2011). https://doi.org/10.1038/nature10388
  2. Cesar A, Murray BE, "Antibiotic-Resistant Bugs in the 21st Century - A Clinical Super-Challenge," New England Journal of Medicine, 360(5), 439-443 (2009). https://doi.org/10.1056/NEJMp0804651
  3. Fjell CD. Hiss JA. Hancock REW, Schneider G, "Designing antimicrobial peptides: Form follows function," Nat. Rev. Drug Discovery 11, 3751 (2012).
  4. Fjell CD. Hiss JA. Hancock REW, Schneider G, "Designing antimicrobial peptides: Form follows function.," Nat. Rev. Drug Discovery 11, 37-51 (2012).
  5. Epand R M, Vogel HJ, "Diversity of antimicrobial peptides and their mechanisms of action," Biochim. Biophys. Acta 1462, 11-28, (1999). https://doi.org/10.1016/S0005-2736(99)00198-4
  6. Hancock REW, Sahl HG, "Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies," Nat. Biotechnol. 24, 1551-1557 (2006). https://doi.org/10.1038/nbt1267
  7. Yeaman MR, Yount NY, "Mechanisms of antimicrobial peptide action and resistance," Pharmacol. Rev. 55, 27-55 (2003). https://doi.org/10.1124/pr.55.1.2
  8. Zasloff M, "Antimicrobial peptides of multicellular organisms," Nature 415, 389-395 (2002). https://doi.org/10.1038/415389a
  9. van't HW, Veerman EC. Helmerhorst EJ. Amerongen AV, "Antimicrobial peptides: properties and applicability," The Journal of Biological Chemistry, 382(4), 597-619, (2001).
  10. Hancock RE, Lehrer R, "Cationic peptides: a new source of antibiotics," Trends in Biotechnology, 16(2), 82-88 (1998). https://doi.org/10.1016/S0167-7799(97)01156-6
  11. Christine C, Viviane SP, Catherine M, Pascal S, "Antibacterial Peptides: A Review," Science against microbial pathogens: communicating current research and technological advances, A. Mendez-Vilas (Ed.), 926-937" (2011).
  12. Matsuzaki K. Sugishita K. Fujii N, Miyajima K., "Molecular-basis for membrane selectivity of an antimicrobial peptide, magainin-2," Biochemistry 34, 3423.3429 (1995). https://doi.org/10.1021/bi00010a034
  13. Glukhov E, Stark M. Burrows LL, Deber CM, "Basis for selectivity of cationic antimicrobial peptides for bacterial versus mammalian membranes." J. Biol. Chem. 280, 33960-33967 (2005). https://doi.org/10.1074/jbc.M507042200
  14. Shai, Y. "Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by $\alpha$-helical antimicrobial and cell non-selective membrane-lytic peptides," Biochim. Biophys. Acta, 1462, 55-70 (1999). https://doi.org/10.1016/S0005-2736(99)00200-X
  15. Maloy WL, Kari UP, "Structure-activity studies on magainins and other host-defense peptides," Biopolymers, 37, 105, 122 (1995). https://doi.org/10.1002/bip.360370206
  16. Gottler LM, Ramamoorthy A, "Structure, membrane orientation, mechanism, and function of pexiganan: A highly potent antimicrobial peptide designed from magainin," Biochim. Biophys. Acta 1788, 1680-1686 (2009). https://doi.org/10.1016/j.bbamem.2008.10.009
  17. Pouny Y, Rapaport D, Mor A, Nicolas P, Shai Y, "Interaction of antimicrobial dermaseptin and its fluorescently labeled analogues with phospholipid membranes," Biochemistry, 15, 31(49), 12416-23 (1992). https://doi.org/10.1021/bi00164a017
  18. Steve J, Ludtke KH, William TH, Thad AH, Lin Y, Huey WH, "Membrane Pores Induced by Magainin," Biochemistry 35, 13723-13728 (1996). https://doi.org/10.1021/bi9620621
  19. Ehrenstein G, Lecar H, "Electrically gated ionic channels in lipid bilayers," Q Rev Biophys, 10(1), 1-34 (1977). https://doi.org/10.1017/S0033583500000123
  20. Trantas E, Panopoulos N, Ververidis F, "Metabolic engineering of the complete pathway leading to heterologous biosynthesis of various flavonoids and stilbenoids in Saccharomyces cerevisiae," Metab. Eng, 11(6), 355-66 (2009). https://doi.org/10.1016/j.ymben.2009.07.004
  21. Lipsky B A. Holroyd K. J, Zasloff M, "Topical versus systemic antimicrobial therapy for treating mildly infected diabetic foot ulcers: A randomized, controlled, double-blinded, multicenter trial of pexiganan cream," Clin. Infect. Dis. 47, 1537, 1545 (2008). https://doi.org/10.1086/593185
  22. Kevin JH, Lee DK, and Ramamoorthy A, "MSI-78, an Analogue of the Magainin Antimicrobial Peptides, Disrupts Lipid Bilayer Structure via Positive Curvature Strain," Biophysical Journal, 84, 3052-3060 (2003). https://doi.org/10.1016/S0006-3495(03)70031-9
  23. Lee DK, Brender JR, Sciacca MFM, Krishnamoorthy J, Yu CS, Ramamoorthy A, "Lipid Composition-Dependent Membrane Fragmentation and Pore-Forming Mechanisms of Membrane Disruption by Pexiganan (MSI-78)," Biochemistry, 52, 32543263 (2013). https://doi.org/10.1021/bi400087n
  24. Morein S, Andersson A, Rilfors L, Lindblom G, "Wild-type Escherichia coli cells regulate the membrane lipid composition in a "window" between gel and non-lamellar structures," J Biol Chem, 271(12), 6801-6809 (1996). https://doi.org/10.1074/jbc.271.12.6801
  25. Virtanen JA, Cheng KH, Somerharju P, "Phospholipid composition of the mammalian red cell membrane can be rationalized by a superlattice model." Proc. Natl. Acad. Sci. USA, 95, 4964-4969 (1998). https://doi.org/10.1073/pnas.95.9.4964
  26. Maloy WL, Kari UP, "Structure-activity studies on magainins and other host-defense peptides," Biopolymers, 37, 105-122 (1995). https://doi.org/10.1002/bip.360370206
  27. Kresten B, Jerzy D, Sara KH, Niels CN, Thomas V, "Mechanisms of Peptide-Induced Pore Formation in Lipid Bilayers Investigated by Oriented 31P Solid-State NMR Spectroscopy," PLOS ONE, 7(10), e47745 (2012). https://doi.org/10.1371/journal.pone.0047745
  28. Porcelli F, Verardi R, Shi L, Henzler-Wildman KA, Ramamoorthy A, Veglia G., "NMR Structure of the Cathelicidin-Derived Human Antimicrobial Peptide LL-37 in Dodecylphosphocholine Micelles," Biochemistry, 47(20), 5565-5572 (2008). https://doi.org/10.1021/bi702036s
  29. Fitzroy JB, Helim AE, Victor G, Romanenko G, Rothblat H, Irena L, "Cholesterol Depletion Increases Membrane Stiffness of Aortic Endothelial Cells," Biophysical Journal 87, 3336-3343 (2004). https://doi.org/10.1529/biophysj.104.040634
  30. Chen G, Chen Y, Yang N, Zhu X, Sun L, Li G, "Interaction between curcumin and mimetic biomembrane," Sci China Life Sci, 55(6), 527-32 (2012).