Design of potent 9-mer antimicrobial peptide analogs of protaetiamycine and investigation of mechanism of antimicrobial action

Journal of Peptide Science

Volumn 15, Issue 9, 2009, Pages 559-568

  Shin, Soyoung ^a   Kim, Jin Kyoung ^a   Lee, Jee Young ^a   Jung, Ki Woong ^a   Hwang, Jae Sam ^b   Lee, Juneyoung ^c   Lee, Dong Gun ^c   Kim, Iksoo ^d   Shin, Song Yub ^e   Kim, Yangmee ^a  

^a Konkuk University   (South Korea)

^b National Institute of Animal Science   (South Korea)

^c Kyungpook National University   (South Korea)

^d Chonnam National University   (South Korea)

^e Chosun University   (South Korea)

Author keywords

Antimicrobial peptide; Bacterial cell selectivity; Intracellular mechanism; Protaetiamycine analogs

Indexed keywords

ARGININE; ARGINYLLEUCYLARGINYLARGINYLISOLEUCYLGLYCYLARGINYLARGINYL AMIDE; ARGINYLLEUCYLTRYPTOPHANYLALANYLISOLEUCYLGLYCYLARGINYLGLYCYL AMIDE DERIVATIVE; ARGINYLLEUCYLTYROSYLLEUCYLARGINYLISOLEUCYLGLYCYLARGINYLARGINYL AMIDE; GLYCINE; ISOLEUCINE; LYSINE; MELITTIN; POLYPEPTIDE ANTIBIOTIC AGENT; UNCLASSIFIED DRUG;

AMINO ACID SUBSTITUTION; ANTIBACTERIAL ACTIVITY; ANTIBIOTIC RESISTANCE; BACTERIAL MEMBRANE; BINDING AFFINITY; CELL MEMBRANE DEPOLARIZATION; CONFERENCE PAPER; CONTROLLED STUDY; CYTOTOXICITY TEST; DRUG DESIGN; DRUG DNA BINDING; DRUG EFFICACY; DRUG STRUCTURE; HUMAN; HUMAN CELL; HYDROPHOBICITY; MEMBRANE PERMEABILITY; MEMBRANE POTENTIAL; MINIMUM INHIBITORY CONCENTRATION; NONHUMAN; PHOSPHOLIPID MEMBRANE; PRIORITY JOURNAL; STAPHYLOCOCCUS AUREUS;

AMINO ACID SEQUENCE; ANTIMICROBIAL CATIONIC PEPTIDES; CELL PROLIFERATION; CELLS, CULTURED; CIRCULAR DICHROISM; DNA; HEMOLYSIS; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; MICROBIAL SENSITIVITY TESTS; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; STRUCTURE-ACTIVITY RELATIONSHIP;

BACTERIA (MICROORGANISMS); CANDIDA ALBICANS; COLEOPTERA; HEXAPODA; MAMMALIA; PROTAETIA BREVITARSIS; STAPHYLOCOCCUS AUREUS;

EID: 70349637846     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.1156     Document Type: Conference Paper

References (45)

1. Hwang J, Kang B, Kim SR, Yun E, Park K, Jeon JP, Nam S, Suh H, Hong MY,Kim I. Molecular characterization of adefensin-like-peptide from larvae of a beetle, Protaetia brevitarsis. Int. J. Ind. Entomol. 2008; 17: 131-135.
2. Boman HG. Peptide antibiotics and their role in innate immunity. Annu. Rev. Immunol. 1995; 13: 61-92.
3. Hancock RE, Lehrer R. Cationic peptides: a new source of antibiotics. Trends Biotechnol. 1998; 16: 82-88.
4. Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 2002; 415: 389-395.
5. EpandRM, Vogel HJ. Diversity of antimicrobial peptides and their mechanisms of action. Biochim. Biophys. Acta 1999; 1462: 11-28.
6. Hancock RE, Rozek A. Role of membranes in the activities of antimicrobial cationic peptides. FEMS Microbiol. Lett. 2002; 206: 143-149.
7. Otvos L Jr. Antibacterial peptides isolated from insects. J. Pept. Sci. 2000; 6: 497-511.
8. Dimarcq JL, Bulet P, Hetru C, Hoffmann J. Cysteine-richantimicrobial peptides in invertebrates. Biopolymers 1998; 47: 465-477.
9. Lopez L, Morales G, Ursic R, Wolff M, Lowneberger C. Isolation and characterization of a novel insect defensin from Rhodnius prolixus, a vector of Chagas disease. Insect Biochem. Mol. Biol. 2003; 33: 439-447.
10. Hultmark D. Drosophila immunity: paths and patterns. Curr. Opin. Immunol. 2003; 15: 12-19.
11. Hoffmann JA. The immune response of Drosophila. Nature 2003; 426: 33-38.
12. Lemaitre B. The road to toll. Nat. Rev. Immunol. 2004; 4: 521-527.
13. Hoffman JA, Kafatos FC, Janeway CA, Ezekowitz RA. Phylogenic perspectives in innate immunity. Science 1999; 284: 1313-1318.
14. Engstrom Y. Induction and regulation of antimicrobial peptides in Drosophila. Dev. Comp. Immunol. 1999; 23: 345-358.
15. Bulet P, Hetru C, Dimarcq JL, Hoffmann D. Antimicrobial peptides in insects: structure and function. Dev. Comp. Immunol. 1999; 23: 329-344.
16. Hultmark D. Immune reactions in Drosophila and other insects: a model for innate immunity. Trends Genet. 1993; 9: 178-183.
17. Volkoff AN, Rocher J, d'Alencon E, Bouton M, Landais I, Quesada-Moraga E, Vey A, Fournier P, Mita K, Devauchelle G. Characterization and transcriptional profiles of three Spodoptera frugiperdagenes encoding cysteine-rich peptides. A new class of defensin-like genes from lepidopteran insects? Gene 2003; 319: 43-53.
18. Taylor K, Barran PE, Dorin JR. Structure-activity relationships in β-defensin peptides. Biopolymers 2008; 90: 1-7.
19. Hopp TP, Woods KR. Prediction of protein antigenic determinants from amino acid sequences. Proc. Natl. Acad. Sci. USA 1981; 78: 3824-3828.
20. Shai Y, Bach D, Yanovsky A. Channel formation properties of synthetic pardaxin and analogues. J. Biol. Chem. 1990; 265: 20202-20209.
21. Mao D, Wallace BA. Differential light scattering and absorption flattening optical effects are minimal in the circular-dichroism spectra of small unilamellar vesicles. Biochemistry 1984; 23: 2667-2673.
22. Zhao H, Kinnunen PK. Binding of the antimicrobial peptide temporin L to liposomes assessed by Trp fluorescence. J. Biol. Chem. 2002; 277: 25170-25177.
23. Friedrich CL, Moyles D, Beveridge TJ, Hancock RE. Antibacterial action of structurally diverse cationic peptides on Gram-positive bacteria. Antimicrob. Agents Chemother. 2000; 44: 2086-2092.
24. Park CB, Kim HS, Kim SC. 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. 1998; 244: 253-257.
25. Marion D, Wüthrich K. Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins. Biochem. Biophys. Res. Commun. 1983; 113: 967-974.
26. Derome A, Williamson M. Rapid-pulsing artifacts in doublequantum-filtered COSY. J. Magn. Reson. 1990; 88: 177-185.
27. Bax A, Davis DG. Practical aspects of two-dimensional transverse NOE spectroscopy. J. Magn. Reson. 1985; 63: 207-213.
28. Bax A, Davis DG. MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J. Magn. Reson. 1985; 65: 355-360.
29. Delaglio F, Grzesiak S, Vuister G, Zhu G, Pfeifer J, BaxA. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 1995; 6: 277-293.
30. Goddard T, Kneller DG. SPARKY3, University of California: San Francisco.
31. Saido-Sakanaka H, Ishibashi J, Sagisaka A, Momotani E, Yamakawa M. Synthesis and characterization of bactericidal oligopeptides designed on the basis of an insect anti-bacterial peptide. Biochem. J. 1999; 338: 29-33.
32. Yamada M, Nakamura K, Saido-Sakanaka H, Asaoka A, Yamakawa M, Yamamoto Y, Koyama Y, Hikosaka K, Shimizu A, Hirota Y. Therapeutic effect of modified oligopeptides from the beetle Allomyrina dichotoma on methicillin-resistant Staphylococcusaureus (MRSA) infection in mice. J. Vet. Med. Sci. 2005; 67: 1005-1011.
33. Koyama Y, Motobu M, Hikosaka K, Yamada M, Nakamura K, Saido-Sakanaka H, Asaoka A, Yamakawa M, Isobe T, Shimura K, Kang CB, Hayashidani H, Nakai Y, Hirota Y. Cytotoxicity and antigenicity of antimicrobial synthesized peptides derived from the beetle Allomyrina dichotoma defensin in mice. Int. Immunopharmacol. 2006; 6: 1748-1753.
34. Ghosh AK, Rukmini R, Chattopadhyay A. Modulation of tryptophan environment in membrane-bound melittin by negatively charged phospholipids: implications in membrane organization and function. Biochemistry 1997; 36: 14291-14305.
35. Yu K, Kang S, Park N, Shin J, Kim Y. Relationship between the tertiary structures of mastoparan B and its analogs and their lytic activities studied by NMR spectroscopy. J. Pept. Res. 2000; 55: 51-65.
36. Lee K, Shin SY, Kim K, Lim SS, Hahm KS, Kim Y. Antibiotic activity and structural analysis of the scorpion-derived antimicrobial peptide IsCT and its analogs. Biochem. Biophys. Res. Commun. 2004; 323: 712-719.
37. Orioni B, Bocchinfuso G, Kim JY, Palleschi A, Grande G, Bobone S, Park Y, Kim JI, Hahm K-S, Stella L. Membrane perturbation by the antimicrobial peptide PMAP-23: a fluorescence and molecular dynamics study. Biochim. Biophys. Acta 2009; 1788: 1523-1533.
38. Park CB, Yi KS, Matsuzaki K, Kim MS, Kim SC. Structure-activity analysis of buforin II, a histone H2A-derived antimicrobial peptide: the proline hinge is responsible for the cell-penetrating ability of buforin II. Proc. Natl. Acad. Sci. USA 2000; 97: 8245-8250.
39. Cudic M, Otvos L Jr. Intracellular targets of antibacterial peptides. Curr. Drug Targets 2000; 3: 101-106.
40. Woody RW. Contributions of tryptophan side chains to the farultra-violet circular dichroism of proteins. Eur. Biophys J. 1994; 23: 253-262.
41. Woody RW. Peptides, Polypeptides, and Proteins. Wiley: New York, 1974.
42. Ladokhin AS, Selsted ME, White SH. CD spectra of indolicidin antimicrobial peptides suggest turns, not polyproline helix. Biochemistry 1999; 38: 12313-12319.
43. Damberg P, Jarvet J, Graslund A. Micellar systems as solvents in peptide and protein structure determination. Methods Enzymol. 2001; 339: 271-285.
44. Campagna S, Saint N,Molle G, Aumelas A. Structure and mechanism of action of the antimicrobial peptide piscidin. Biochemistry 2007; 46: 1771-1778.
45. Wüthrich K. NMR of Proteins and Nucleic Acids. Wiley: New York, 1986.