Selectivity in the mechanism of action of antimicrobial mastoparan peptide Polybia-MP1

European Biophysics Journal

Volumn 37, Issue 6, 2008, Pages 879-891

  Dos Santos Cabrera, Marcia Perez ^a,b   Costa, Sabrina Thais Broggio ^a   De Souza, Bibiana Monson ^a   Palma, Mario Sérgio ^a   Ruggiero, José Roberto ^a   Ruggiero Neto, João ^a  

^a SÃO PAULO STATE UNIVERSITY UNESP   (Brazil)

^b UNIVERSITY OF SÃO PAULO   (Brazil)

Author keywords

Cationic antimicrobial peptide; Conformational analysis; Hydrophobicity; Lytic activity and cooperativity; Selectivity; Wasp venom mastoparan

Indexed keywords

ASPARTIC ACID DERIVATIVE; MASTOPARAN; POLYBIA MP1; POLYPEPTIDE ANTIBIOTIC AGENT; SOLVENT;

ALPHA HELIX; ARTICLE; CIRCULAR DICHROISM; DRUG MECHANISM; ELECTRICITY; ENVIRONMENT; HEMOLYSIS; HYDROPHILICITY; MOLECULAR DYNAMICS; PROTEIN STRUCTURE; SIMULATION; SOLVATION;

ANTI-INFECTIVE AGENTS; COMPUTER SIMULATION; DIFFUSION; LIPID BILAYERS; LIPOSOMES; MODELS, CHEMICAL; MODELS, MOLECULAR; PEPTIDES; POROSITY; PROTEIN CONFORMATION; WASP VENOMS;

BACTERIA (MICROORGANISMS); POLYBIA; POLYBIA PAULISTA;

EID: 45849143289     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00249-008-0299-7     Document Type: Article

References (56)

1. Allende D, McIntosh TJ (2003) Lipopolysaccharides in bacterial membranes act like cholesterol in eukaryotic plasma membranes in providing protection against melittin-induced bilayer lysis. Biochemistry 42:1101-1108
2. Allende D, Simon SA, McIntosh TJ (2005) Melittin-induced bilayer leakage depends on lipid material properties: evidence for toroidal pores. Biophys J 88:1828-1837
3. Andersson A, Danielsson J, Graslund A, Maler L (2007) Kinetic models for peptide-induced leakage from vesicles and cells. Eur Biophys J 36:621-635
4. Berendsen HJC, Postma JPM, van Gunsteren WF, Hermans J (1981) Interaction models for water in relation to protein hydration. In: Pullman B (ed) Intermolecular forces. Reidel, Dordrecht, pp 331-342
5. Berendsen HJC, Postma JPM, van Gunsteren W, Di Nola A, Haak JRJ (1984) Molecular dynamics with coupling to an external bath. J Chem Phys 81:3684-3690
6. Brochard-Wyart F, de Gennes PG, Sandre O (2000) Transient pores in stretched vesicles: role of leak-out. Physica A 278:32-51
7. Cheatham TE III, Miller JL, Fox T, Darden TA, Kollman PA (1995) Molecular dynamics simulations on solvated biomolecular system: The Particle Mesh Ewald method leads to stable trajectories of DNA, RNA, and proteins. J Am Chem Soc 117:4193-4194
8. Chen FY, Lee MT, Huang HW (2003) Evidence for membrane thinning effect as the mechanism for peptide-induced pore formation. Biophys J 84:3751-3758
9. Chuang CC, Huang WC, Yu HM, Wang KT, Wu SH (1996) Conformation of Vespa basalis Mastoparan-B in trifluoroethanol-containing aqueous solution. Biochim Biophys Acta 1292:1-8
10. Dathe M, Schumann M, Wieprecht T, Winkler A, Beyermann M, Krause E, Matsuzaki K, Murase O, Bienert M (1996) Peptide helicity and membrane surface charge modulate the balance of electrostatic and hydrophobic interactions with lipid bilayers and biological membranes. Biochemistry 35:12612-12622
11. Dathe M, Wieprecht T, Nikolenko H, Handel L, Maloy WL, MacDonald DL, Beyermann M, Bienert M (1997) Hydrophobicity, hydrophobic moment and angle subtended by charged residues modulate antibacterial and haemolytic activity of amphipathic helical peptides. FEBS Lett 403:208-212
12. Dathe M, Nikolenko H, Meyer J, Beyermann M, Bienert M (2001) Optimization of the antimicrobial activity of Magainin peptides by modification of charge. FEBS Lett 501:146-150
13. Dos Santos Cabrera MP, de Souza BM, Fontana R, Konno K, Palma MS, de Azevedo Jr WF, Ruggiero Neto J (2004) Conformation and lytic activity of Eumenine Mastoparan: a new antimicrobial peptide from wasp venom. J Peptide Res 64:95-103
14. Eisenberg D, Schwarz E, Komaromy M, Wall R (1984) Analysis of membrane and surface protein sequences with the hydrophobic moment plot. J Mol Biol 179:125-142
15. Fioroni M, Burger K, Mark AE, Roccatano D (2000) A new 2,2,2-trifluoroethanol model for molecular dynamics simulations. J Phys Chem B 104:12347-12354
16. Haines TH, Dencher NA (2002) Cardiolipin: a proton trap for oxidative phosphorylation. FEBS Lett 528:35-39
17. Heerklotz H, Seelig J (2007) Leakage and lysis of lipid membranes induced by the lipopeptide surfactin. Eur Biophys J 36:305-314
18. Hess B, Bekker H, Berendsen HJC, Fraaije JGE (1997) LINCS: a linear constraint solver for molecular simulations. J Comp Chem 18:1463-1472
19. 0 by Mastoparan, related amphiphilic peptides and hydrophobic amines. J Biol Chem 265:14176-14186
20. Hirai Y, Kuwada M, Yasuhara T, Yoshida H, Nakajima T (1979a) A new mast cell degranulating peptide homologous to mastoparan in the venom of Japanese hornet (Vespa xanthoptera). Chem Pharm Bull (Tokyo) 27:1945-1946
21. Hirai Y, Yasuhara T, Yoshida H, Nakajima T, Fujino M, Kitada C (1979b) A new mast cell degranulating peptide "mastoparan" in the venom of Vespula lewisii. Chem Pharm Bull (Tokyo) 27:1942-1944
22. Hori Y, Demura M, Iwadate M, Ulrich AS, Niidome T, Aoyagi H, Asakura T (2001) Interaction of mastoparan with membranes studied by 1H-NMR spectroscopy in detergent micelles and by solid-state 2H-NMR and 15N-NMR spectroscopy in oriented lipid bilayers. Eur J Biochem 268:302-309
23. Huang HW (2000) Action of antimicrobial peptides: two-state model. Biochemistry 39:8347-8352
24. Konno K, Hisada M, Naoki H, Itagaki Y, Kawai N, Miwa A, Yasuhara T, Morimoto Y, Nakata Y (2000) Structure and biological activities of Eumenine Mastoparan-AF (EMP-AF), a new mast cell degranulating peptide in the venom of the solitary wasp (Anterhynchium flavomarginatum micado). Toxicon 38:1505-1515
25. Konno K, Hisada M, Fontana R, Lorenzi CCB, Naoki H, Itagaki Y, Miwa A, Kawai N, Nakata Y, Yasuhara T, Ruggiero Neto J, Azevedo Jr WF, Palma MS, Nakajima T (2001) Anoplin, a novel antimicrobial peptide from the venom of the solitary wasp Anoplius samariensis. Biochim Biophys Acta 1550:70-80
26. Kusunoki H, Wakamatsu K, Sato K, Miyazawa T, Kohno T (1998) G protein-bound conformation of mastoparan-X: heteronuclear multidimensional transferred nuclear overhauser effect analysis of peptide uniformly enriched with 13C and 15N. Biochemistry 37:4782-4790
27. Ladokhin AS, Selsted ME, White SH (1997) Bilayer interactions of Indolicidin, a small antimicrobial peptide rich in tryptophan, proline, and basic amino acids. Biophys J 72:794-805
28. Ladokhin AS, Jayasinghe S, White SH (2000) How to measure and analyze tryptophan fluorescence in membranes properly, and why bother? Anal Biochem 285:235-245
29. Lange Y, Dolde J, Steck TL (1981) The rate of transmembrane movement of cholesterol in the human erythrocyte. J Biol Chem 256:5321-5323
30. Lee MT, Hung WC, Chen FY, Huang HW (2005) Many-body effect of antimicrobial peptides: on the correlation between lipid's spontaneous curvature and pore formation. Biophys J 89:4006-4016
31. Lindahal E, Hess B, van der Spoel D (2001) Gromacs 3.0: a package for molecular simulations and trajectory analysis. J Mol Model 7:306-317
32. Lohner K, Prenner EJ (1999) Differential scanning calorimetry and X-ray diffraction studies of the specificity of the interaction of antimicrobial peptides with membrane-mimetic systems. Biochim Biophys Acta 1462:141-156
33. Matsuzaki K (1999) Why and how are peptide-lipid interactions utilized for self-defense? Magainins and Tachyplesins as archetypes. Biochim Biophys Acta 1462:1-10
34. Matsuzaki K, Yoneyama S, Murase O, Miyajima K (1996) Transbilayer transport of ions and lipids coupled with mastoparan X translocation. Biochemistry 35:8450-8456
35. Matsuzaki K, Sugishita K, Ishibe N, Ueha M, Nakata S, Miyajima K, Epand RM (1998) Relationship of membrane curvature to the formation of pores by Magainin 2. Biochemistry 37:11856-11863
36. McDowell L, Sanyal GB, Prendergast FG (1985) Probable role of amphiphilicity in the binding of mastoparan to calmodulin. Biochemistry 24:2979-2984
37. Mendes MA, de Souza BM, Palma MS (2005) Structural and biological characterization of three novel mastoparan peptides from the venom of the neotropical social wasp Protopolybia exigua (Saussure). Toxicon 45:101-106
38. Miyamoto S, Kollman PA (1992) SETTLE: an analytical version of the SHAKE and RATTLE algorithm for rigid water models. J Comput Chem 13:952-962
39. Nakajima T, Uzu S, Wakamatsu K, Saito K, Miyazawa T, Yasuhara T, Tsukamoto Y, Fujino M (1986) Amphiphilic peptides in wasp venom. Biopolymers 25:115-121
40. Needham D, Nunn RS (1990) Elastic deformation and failure of lipid bilayer membranes containing cholesterol. Biophys J 58:997-1009
41. Park NG, Yamato Y, Lee S, Sugihara G (1995) Interaction of Mastoparan-B from venom of a hornet in Taiwan with phospholipid bilayer and its antimicrobial activity. Biopolymers 36:793-801
42. Rohl CA, Baldwin RL (1998) Deciphering rules of helix stability in peptides. Methods Enzymol 295:1-26
43. Rouser G, Fleischer S, Yamamoto A (1970) Two dimensional thin layer chromatographic separation of polar lipids and determination of phospholipids by phosphorus analysis of spots. Lipids 5:494-496
44. Schwarz G, Robert CH (1990) Pore formation kinetics in membranes, determined from the release of marker molecules out of liposomes or cells. Biophys J 58:577-583
45. Schwarz G, Blochmann U (1993) Association of the wasp venom peptide mastoparan with electrically neutral lipid vesicles-salt effects on partitioning and conformational state. FEBS Lett 318:172-176
46. Shay Y (1999) 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
47. Shoemaker KR, Kim PS, Brems DN, Marqusee S, York EJ, Chaiken IM, Stewart JM Baldwin RL (1985) Nature of the charged-group effect on the stability of the C-peptide helix. PNAS 82:2349-2353
48. Souza BM (2007) Estrutura e função de mastoparanos dos venenos de vespas (PhD thesis in Cellular and Molecular Biology) Instituto de Biociências de Rio Claro, UNESP-Universidade Estadual Paulista, Rio Claro, Brasil
49. Souza BM, Mendes MA, Santos LD, Marques MR, Cesar LM, Almeida RN, Pagnocca FC, Konno K, Palma MS (2005) Structural and functional characterization of two novel peptide toxins isolated from the venom of the social wasp Polybia paulista. Peptides 26:2157-2164
50. Taheri-Araghi S, Ha BY (2007) Physical basis for membrane-charge selectivity of cationic antimicrobial peptides. Phys Rev Lett 98:168101
51. van Gunsteren WF, Billeter SR, Eising AA, Hünenberger PH, Krüger P, Mark AE, Scott WRP, Tironi IG (1996) Biomolecular simulation: the GROMOS96 manual and user guide; vdf Hochschulverlang: ETH Zürich, Switzerland
52. Wakamatsu K, Okada A, Miyazawa T, Ohya M, Higashijima T (1992) Membrane-bound conformation of Mastoparan-X, a G-protein-activating peptide. Biochemistry 3:5654-5660
53. Yeaman MR, Yount NY (2003) Mechanisms of antimicrobial peptide action and resistance. Pharmacol Rev 55:27-55
54. Yu K, Kang S, Park N, Shin J, Kim Y (2000) Relationship between the tertiary structures of mastoparan B and its analogs and their lytic activities studied by NMR spectroscopy. J Pept Res 55:51-62
55. Zasloff M (2002) Antimicrobial peptides of multicellular organisms. Nature 415:389-395
56. Zhao H, Rinaldi AC, Di Giulio A, Simmaco M, Kinnunen PK (2002) Interactions of the antimicrobial peptides temporins with model biomembranes. Comparison of temporins B and L. Biochemistry 41:4425-4436