Expression, purification and structural studies of a short antimicrobial peptide

Biochimica et Biophysica Acta - Biomembranes

Volumn 1788, Issue 2, 2009, Pages 314-323

  Zorko, Mateja ^a   Japelj, Boštjan ^a   Hafner Bratkovič, Iva ^a   Jerala, Roman ^a  

^a NATIONAL INSTITUTE OF CHEMISTRY   (Slovenia)

Author keywords

Antimicrobial peptide; Fluorescence; Lipid membrane; NMR spectroscopy; Recombinant peptide; Solution structure

Indexed keywords

AMPHOLYTE; ASPARTIC ACID; CATION; DODECYL SULFATE SODIUM; DODECYLPHOSPHORYLCHOLINE; HYBRID PROTEIN; LIPOPOLYSACCHARIDE; MACROPHAGE ACTIVATING FACTOR; POLYPEPTIDE ANTIBIOTIC AGENT; PROLINE; PROLYLPHENYLALANYLTRYPTOPHANYLARGINYLISOLEUCYLARGINYLISOLEUCYLARGINYLARGININE; STEROID DELTA ISOMERASE; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ANTIBACTERIAL ACTIVITY; ARTICLE; CONTROLLED STUDY; DRUG ACTIVITY; ESCHERICHIA COLI; FLUORESCENCE; HYDROPHOBICITY; ISOTHERMAL TITRATION CALORIMETRY; MICELLE; MOUSE; NONHUMAN; PH MEASUREMENT; PHOSPHOLIPID VESICLE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CLEAVAGE; PROTEIN EXPRESSION; PROTEIN PURIFICATION; PROTEIN STRUCTURE;

AMINO ACID SEQUENCE; ANIMALS; ANTI-BACTERIAL AGENTS; CALORIMETRY; CELL LINE; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; ESCHERICHIA COLI; GENE EXPRESSION; LIPIDS; MASS SPECTROMETRY; MICE; MICELLES; MODELS, MOLECULAR; PEPTIDES; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SPECTROPHOTOMETRY;

EID: 59249083736     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2008.10.015     Document Type: Article

References (61)

1. Brogden K.A. Antimicrobial peptides: pore formers or metabolic inhibitors in bacteria?. Nat. Rev., Microbiol. 3 (2005) 238-250
2. Boman H.G. Peptide antibiotics and their role in innate immunity. Annu. Rev. Immunol. 13 (1995) 61-92
3. Hancock R.E.W., and Lehrer R. Cationic peptides: a new source of antibiotics. Trends Biotechnol. 16 (1998) 82-88
4. Pag U., Oedenkoven M., Sass V., Shai Y., Shamova O., Antcheva N., Tossi A., and Sahl H.G. Analysis of in vitro activities and modes of action of synthetic antimicrobial peptides derived from an alpha-helical 'sequence template'. J. Antimicrob. Chemother. 61 (2008) 341-352
5. Lehrer R.I., Lichtenstein A.K., and Ganz T. Defensins - antimicrobial and cytotoxic peptides of mammalian-cells. Annu. Rev. Immunol. 11 (1993) 105-128
6. Hilpert K., Volkmer-Engert R., Walter T., and Hancock R.E.W. High-throughput generation of small antibacterial peptides with improved activity. Nat. Biotechnol. 23 (2005) 1008-1012
7. Rosenfeld Y., Papo N., and Shai Y. Endotoxin (lipopolysaccharide) neutralization by innate immunity host-defense peptides - peptide properties and plausible modes of action. J. Biol. Chem. 281 (2006) 1636-1643
8. Park C.B., Kim H.S., and Kim S.C. Mechanism of action of the antimicrobial peptide buforin II: buforin II kills microorganisms by penetrating the cell membrane and inhibiting cellular functions. Biochem. Biophys. Res. Commun. 244 (1998) 253-257
9. Kim H.K., Chun D.S., Kim J.S., Yun C.H., Lee J.H., Hong S.K., and Kang D.K. Expression of the cationic antimicrobial peptide lactoferricin fused with the anionic peptide in Escherichia coli. Appl. Microbiol. Biotechnol. 72 (2006) 330-338
10. Cipakova I., Gasperik J., and Hostinova E. Expression and purification of human antimicrobial peptide, dermcidin, in Escherichia coli. Protein Expression Purif. 45 (2006) 269-274
11. Hara S., and Yamakawa M. Production in Escherichia coli of moricin, a novel type antibacterial peptide from the silkworm, Bombyx mori. (vol 220, pg 664, 1996). Biochem. Biophys. Res. Commun. 224 (1996) 877-878
12. Cipakova I., Hostinova E., Gasperik J.G., and Velebny V. High-level expression and purification of a recombinant hBD-1 fused to LMM protein in Escherichia coli. Protein Expression Purif. 37 (2004) 207-212
13. Xu Z.N., Peng L., Zhong Z.X., Fang X.M., and Cen P.L. High-level expression of a soluble functional antimicrobial peptide, human beta-defensin 2, in Escherichia coli. Biotechnol. Prog. 22 (2006) 382-386
14. Xu Z., Zhong Z.X., Huang L., Peng L., Wang F., and Cen P. High-level production of bioactive human beta-defensin-4 in Escherichia coli by soluble fusion expression. Appl. Microbiol. Biotechnol. 72 (2006) 471-479
15. Lee J.H., Minn I., Park C.B., and Kim S.C. Acidic peptide-mediated expression of the antimicrobial peptide buforin II as tandem repeats in Escherichia coli. Protein Expression Purif. 12 (1998) 53-60
16. Majerle A., Kidric J., and Jerala R. Production of stable isotope enriched antimicrobial peptides in Escherichia coli: an application to the production of a N-15-enriched fragment of lactoferrin. J. Biomol. NMR 18 (2000) 145-151
17. Mac T.T., Beyermann M., Pires J.R., Schmieder P., and Oschkinat H. High yield expression and purification of isotopically labelled human endothelin-1 for use in NMR studies. Protein Expression Purif. 48 (2006) 253-260
18. Jin F.L., Xu X.X., Zhang W.Q., and Gu D.X. Expression and characterization of a housefly cecropin gene in the methylotrophic yeast, Pichia pastoris. Protein Expression Purif. 49 (2006) 39-46
19. Wei Q.D., Kim Y.S., Seo J.H., Jang W.S., Lee I.H., and Cha H.J. Facilitation of expression and purification of an antimicrobial peptide by fusion with baculoviral polyhedrin in Escherichia coli. Appl. Environ. Microbiol. 71 (2005) 5038-5043
20. Moon J.Y., Henzler-Wildman K.A., and Ramamoorthy A. Expression and purification of a recombinant LL-37 from Escherichia coli. Biochim. Biophys. Acta-Biomembr. 1758 (2006) 1351-1358
21. Xu X.X., Jin F.L., Yu X.Q., Ren S.X., Hu J., and Zhang W.Q. High-level expression of the recombinant hybrid peptide cecropinA(1-8)-magainin2(1-12) with an ubiquitin fusion partner in Escherichia coli. Protein Expression Purif. 55 (2007) 175-182
22. Xu X.X., Jin F.L., Yu X.Q., Ji S.X., Wang J., Cheng H.X., Wang C., and Zhang W.Q. Expression and purification of a recombinant antibacterial peptide, cecropin, from Escherichia coli. Protein Expression Purif. 53 (2007) 293-301
23. Pyo S.H., Lee J.H., Park H.B., Cho J.S., Kim H.R., Han B.H., and Park Y.S. Expression and purification of a recombinant buforin derivative from Escherichia coli. Process Biochem. 39 (2004) 1731-1736
24. Shen Y., Lao X.G., Chen Y., Zhang H.Z., and Xu X.X. High-level expression of cecropin X in Escherichia coli. Int. J. Mol. Sci. 8 (2007) 478-491
25. Ingham A.B., and Moore R.J. Recombinant production of antimicrobial peptides in heterologous microbial systems. Biotechnol. Appl. Biochem. 47 (2007) 1-9
26. Japelj B., Pristovsek P., Majerle A., and Jerala R. Structural origin of endotoxin neutralization and antimicrobial activity of a lactoferrin-based peptide. J. Biol. Chem. 280 (2005) 16955-16961
27. Jerala R., Japelj B., Pristovsek P., and Majerle A. Tertiary structure of lactoferrin peptide in complex with LPS for design of novel endotoxin-neutralizing peptides. Shock 21 (2004) 62
28. Majerle A., Kidric J., and Jerala R. Enhancement of antibacterial and lipopolysaccharide binding activities of a human lactoferrin peptide fragment by the addition of acyl chain. J. Antimicrob. Chemother. 51 (2003) 1159-1165
29. Papo N., and Shai Y. Can we predict biological activity of antimicrobial peptides from their interactions with model phospholipid membranes?. Peptides 24 (2003) 1693-1703
30. Sood R., Domanov Y., and Kinnunen P.K.J. Fluorescent temporin B derivative and its binding to liposomes. J. Fluoresc. 17 (2007) 223-234
31. Chan D.I., Prenner E.J., and Vogel H.J. Tryptophan- and arginine-rich antimicrobial peptides: structures and mechanisms of action. Biochim. Biophys. Acta 1758 (2006) 1184-1202
32. Kuliopulos A., and Walsh C.T. Production, purification, and cleavage of tandem repeats of recombinant peptides. J. Am. Chem. Soc. 116 (1994) 4599-4607
33. Yadav P.N., Liu Z.H., and Rafi M.M. A diarylheptanoid from lesser galangal (Alpinia officinarum) inhibits proinflammatory mediators via inhibition of mitogen-activated protein kinase, p44/42, and transcription factor nuclear factor-kappa B. J. Pharmacol. Exp. Ther. 305 (2003) 925-931
34. Smallcombe S.H., Patt S.L., and Keifer P.A. WET solvent suppression and its applications to LC NMR and high-resolution NMR spectroscopy. J. Magn. Reson., Ser. A 117 2 (1995) 295-303
35. M. Piotto, V. Saudek, V. Sklenar, Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions, 2 (1992) 661.
36. P. Pristovsek, H. Ruterjans, R. Jerala, Semiautomatic sequence-specific assignment of proteins based on the tertiary structure-the program st2nmr, 23 (2002) 335.
37. P. Guntert, W. Braun, K. Wuthrich, Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA, 217 (1991) 517.
38. R.A. Laskowski, J.A. Rullmannn, M.W. MacArthur, R. Kaptein, J.M. Thornton, AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR, 8 (1996) 477.
39. R. Koradi, M. Billeter, K. Wuthrich, MOLMOL: a program for display and analysis of macromolecular structures, 14 (1996) 51.
40. Piszkiew D., Landon M., and Smith E.L. Anomalous cleavage of aspartyl-proline peptide bonds during amino acid sequence determinations. Biochem. Biophys. Res. Commun. 40 (1970) 1173-1178
41. Segalas I., Thai R., Menez R., and Vita C. A particularly labile Asp-Pro bond in the green mamba muscarinic toxin Mtx2 - effect of protein conformation on the rate of cleavage. FEBS Lett. 371 (1995) 171-175
42. Lidell M.E., Johansson M.E.V., and Hansson G.C. An autocatalytic cleavage in the c terminus of the human MUC2 mucin occurs at the low pH of the late secretory pathway. J. Biol. Chem. 278 (2003) 13944-13951
43. Smith E.L., Landon M., Piszkiew D., Brattin W.J., Langley T.J., and Melamed M.D. Bovine liver glutamate dehydrogenase - tentative amino acid sequence - Identification of a reactive lysine - nitration of a specific tyrosine and loss of allosteric inhibition by guanosine triphosphate. Proc. Natl. Acad. Sci. U. S. A. 67 (1970) 724-730
44. Hunter H.N., Jing W.G., Schibli D.J., Trinh T., Park I.Y., Kim S.C., and Vogel H.J. The interactions of antimicrobial peptides derived from lysozyme with model membrane systems. Biochim. Biophys. Acta-Biomembr. 1668 (2005) 175-189
45. Epand R.F., Lehrer R.I., Waring A., Wang W., Maget-Dana R., Lelievre D., and Epand R.M. Direct comparison of membrane interactions of model peptides composed of only Leu and Lys residues. Biopolymers 71 (2003) 2-16
46. Wüthrich K. NMR of Proteins and Nucleic Acids (1986), Wiley & Sons
47. Wishart D.S., Sykes B.D., and Richards F.M. Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J. Mol. Biol. 222 (1991) 311-333
48. Jing W., Svendsen J.S., and Vogel H.J. Comparison of NMR structures and model-membrane interactions of 15-residue antimicrobial peptides derived from bovine lactoferricin. Biochem. Cell Biol. 84 (2006) 312-326
49. Haught C., Davis G.D., Subramanian R., Jackson K.W., and Harrison R.G. Recombinant production and purification of novel antisense antimicrobial peptide in Escherichia coli. Biotechnol. Bioeng. 57 (1998) 55-61
50. Pierce J.C., Maloy W.L., Salvador L., and Dungan C.F. Recombinant expression of the antimicrobial peptide polyphemusin and its activity against the protozoan oyster pathogen Perkinsus marinus. Mol. Mar. Biol. Biotechnol. 6 (1997) 248-259
51. Majerle A., Kidric J., and Jerala R. Production of stable isotope enriched antimicrobial peptides in Escherichia coli: an application to the production of a 15N-enriched fragment of lactoferrin. J. Biomol. NMR 18 (2000) 145-151
52. Pan Y.L., Cheng J.T., Hale J., Pan J., Hancock R.E., and Straus S.K. Characterization of the structure and membrane interaction of the antimicrobial peptides aurein 2.2 and 2.3 from Australian southern bell frogs. Biophys. J. 92 (2007) 2854-2864
53. Yandek L.E., Pokorny A., and Almeida P.F. Small changes in the primary structure of transportan 10 alter the thermodynamics and kinetics of its interaction with phospholipid vesicles. Biochemistry 47 (2008) 3051-3060
54. Schibli D.J., Nguyen L.T., Kernaghan S.D., Rekdal O., and Vogel H.J. Structure-function analysis of tritrpticin analogs: potential relationships between antimicrobial activities, model membrane interactions, and their micelle-bound NMR structures. Biophys. J. 91 (2006) 4413-4426
55. Tossi A., Sandri L., and Giangaspero A. Amphipathic, alpha-helical antimicrobial peptides. Biopolymers 55 (2000) 4-30
56. Wessolowski A., Bienert M., and Dathe M. Antimicrobial activity of arginine- and tryptophan-rich hexapeptides: the effects of aromatic clusters, D-amino acid substitution and cyclization. J. Pept. Res. 64 (2004) 159-169
57. Liu Z., Brady A., Young A., Rasimick B., Chen K., Zhou C., and Kallenbach N.R. Length effects in antimicrobial peptides of the (RW)n series. Antimicrob. Agents Chemother. 51 (2007) 597-603
58. Strom M.B., Haug B.E., Rekdal O., Skar M.L., Stensen W., and Svendsen J.S. Important structural features of 15-residue lactoferricin derivatives and methods for improvement of antimicrobial activity. Biochem. Cell Biol. 80 (2002) 65-74
59. Tang M., Waring A.J., and Hong M. Phosphate-mediated arginine insertion into lipid membranes and pore formation by a cationic membrane peptide from solid-state NMR. J. Am. Chem. Soc. 129 (2007) 11438-11446
60. Japelj B., Zorko M., Majerle A., Pristovsek P., Sanchez-Gomez S., Martinez de Tejada G., Moriyon I., Blondelle S.E., Brandenburg K., Andra J., Lohner K., and Jerala R. The acyl group as the central element of the structural organization of antimicrobial lipopeptide. J. Am. Chem. Soc. 129 (2007) 1022-1023
61. Mitchell J.A., Paul-Clark M.J., Clarke G.W., McMaster S.K., and Cartwright N. Critical role of toll-like receptors and nucleotide oligomerisation domain in the regulation of health and disease. J. Endocrinol. 193 (2007) 323-330