In vitro system for high-throughput screening of random peptide libraries for antimicrobial peptides that recognize bacterial membranes

Journal of Peptide Science

Volumn 12, Issue 10, 2006, Pages 643-652

  Xie, Qiuhong ^a   Matsunaga, Shigeru ^a   Wen, Zhesheng ^a   Niimi, Setsuko ^a   Kumano, Miyuki ^a   Sakakibara, Yoshikiyo ^a   Machida, Sachiko ^a  

^a NATIONAL FOOD RESEARCH INSTITUTE   (Japan)

Author keywords

Antimicrobial peptide; In vitro screening; Model membrane; Peptide library; Phage dispaly; Ribosome display

Indexed keywords

ALANYLLEUCYLARGININE; ALANYLLEUCYLARGINYLALANYLLEUCYLARGINYLALANYLLEUCYLARGINYLALANYLLEUCYLARGINYLALANYLLEUCYLARGININE; ALANYLLEUCYLARGINYLALANYLLEUCYLARGINYLALANYLLEUCYLARGINYLALANYLLEUCYLARGINYLALANYLLEUCYLARGINYLALANYLLEUCYLARGININE; ALANYLLEUCYLARGINYLTYROSYLALANYLLEUCYLARGINYLTYROSYLALANYLLEUCYLARGINYLTYROSYLALANYLLEUCYLARGINYLTYROSYLALANYLLEUCYLARGINYLTYROSINE; ARGINYLCYSTEINYLASPARTYLISOLEUCYLLYSYLSERYLVALYLLYSYLHISTIDYLISOLEUCYLLEUCYLARGINYLCYSTEINYLSERINE; ARGINYLHISTIDYLVALYLPROLYLLYSYLALANYLASPARAGINYLLYSYLGLYCYLALANYLASPARTYLARGINYLSERYLCYSTEINE; ARGINYLVALYLGLYCYLGLYCYLARGINYLVALYLGLYCYLGLYCYLARGINYLVALYLGLYCYLGLYCYLARGINYLVALYLGLYCYLGLYCYLARGINYLVALYLGLYCYLGLYCINE; LYSYLALANYLSERYLVALYLARGINYLASPARAGINYLSERYLLYSYLVALYLLEUCYLPROLYLARGINYLPHENYLALANYLCYSTEINE; LYSYLCYSTEINYLISOLEUCYLALANYLARGINYLARGINYLGLYCYLARGINYLLEUCYLPROLYLVALYLLYSYLARGINYLTYROSINE; LYSYLGLYCYLALANYLPHENYLALANYLARGINYLLEUCYLALANYLLYSYLVALYLLEUCYLISOLEUCYLARGINYLHISTIDYLTYROSINE; LYSYLGLYCYLGLYCYLGLYCYLLYSYLVALYLGLYCYLLYSYLHISTIDYLTHREONYLARGINYLSERYLARGININE; LYSYLSERYLLEUCYLTHREONYLLYSYLCYSTEINYLCYSTEINYLLYSYLVALYLLEUCYLARGINYLLEUCYLSERYLCYSTEINE; LYSYLSERYLVALYLASPARAGINYLLYSYLASPARTYLVALYLARGINYLISOLEUCYLSERYLLEUCYLARGINYLASPARTIC ACID; LYSYLTHREONYLSERYLTRYPTOPHANYLVALYLARGINYLALANYLALANYLALANYLLEUCYLVALYLVALYLVALYLHISTIDINE; LYSYLVALYLLEUCINE; LYSYLVALYLLEUCYLISOLEUCYLASPARAGINYLTRYPTOPHANYLLYSYLGLYCYLISOLEUCYLALANYLALANYLMETHIONYLALANYLLYSYLLYSYLLEUCINE; LYSYLVALYLLEUCYLLYSYLVALYLLEUCYLLYSYLVALYLLEUCINE; LYSYLVALYLLEUCYLLYSYLVALYLLEUCYLLYSYLVALYLLEUCYLLYSYLVALYLLEUCYLLYSYLVALYLLEUCINE; LYSYLVALYLLEUCYLLYSYLVALYLLEUCYLLYSYLVALYLLEUCYLLYSYLVALYLLEUCYLLYSYLVALYLLEUCYLLYSYLVALYLLEUCINE; LYSYLVALYLLEUCYLPHENYLALANYLARGINYLHISTIDYLALANYLARGINYLSERYLSERYLCYSTEINYLLYSYLHISTIDYLTYROSINE; MASTOPARAN; MESSENGER RNA; NUCLEOTIDE; PEPTIDE DERIVATIVE; PEPTIDE LIBRARY; POLYPEPTIDE ANTIBIOTIC AGENT; TRYPTOPHANYLALANYLLEUCYLARGINYLTRYPTOPHANYLALANYLLEUCYLARGINYLTRYPTOPHANYLALANYLLEUCYLARGINYLTRYPTOPHANYLALANYLLEUCYLARGINYLTRYPTOPHANYLALANYLLEUCYLARGININE; UNCLASSIFIED DRUG; UNINDEXED DRUG; VALYLARGINYLASPARAGINYLARGINYLVALYLISOLEUCYLALANYLARGINYLVALYLGLYCYLGLYCYLVALYLPROLYLTYROSYLVALYLGLYCYLGLYCYLPROLYLCYSTEINYLTYROSYLASPARAGINE; VALYLTRYPTOPHANYLASPARAGINYLARGINYLVALYLISOLEUCYLALANYLARGINYLVALYLGLYCYLGLYCYLVALYLLEUCYLTYROSYLVALYLGLYCYLGLYCLPROLYLCYSTEINYLTYROSYLASPARAGINE;

AMINO ACID SEQUENCE; ANTIMICROBIAL ACTIVITY; ARTICLE; BACTERIAL MEMBRANE; COMPLEX FORMATION; CONTROLLED STUDY; CYTOTOXICITY; DISPLAY SYSTEM; DRUG SELECTIVITY; ESCHERICHIA COLI; GENETIC CODE; HIGH THROUGHPUT SCREENING; IMMOBILIZATION; IN VITRO STUDY; INTERMETHOD COMPARISON; ISOLATION PROCEDURE; MAMMAL CELL; MEMBRANE MODEL; MOLECULAR RECOGNITION; NONHUMAN; PHAGE DISPLAY; PRIORITY JOURNAL; PROTEIN MOTIF; RIBOSOME;

AMINO ACID SEQUENCE; ANTI-INFECTIVE AGENTS; BACTERIA; CIRCULAR DICHROISM; COMBINATORIAL CHEMISTRY TECHNIQUES; DRUG EVALUATION, PRECLINICAL; FLUORESCEINS; LIPOSOMES; MEMBRANES, ARTIFICIAL; MOLECULAR SEQUENCE DATA; PEPTIDE LIBRARY; PEPTIDES; RIBOSOMES;

BACTERIA (MICROORGANISMS); MAMMALIA;

EID: 33750077599     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.774     Document Type: Article

References (31)

1. Huttner EM, Bevins CL. Antimicrobial peptides as mediators of epithelial host defense. Pediatr. Res. 1999; 45: 785-794.
2. Barra D, Simmaco M. Amphibian skin: a promising resource for antimicrobial peptides. Trends Biotechnol. 1995; 13: 205-209.
3. Matsuzaki K. Why and how are peptide-lipid interactions utilized for sell-defense? Magainins and tachyplesins as archetypes. Biochim. Biophys. Acta 1999; 1462: 1-10.
4. Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 2002; 415: 389-395.
5. Binder S, Levitt AM, Sacks JJ, Hughes JM. Emerging infectious diseases: public health issues for the 21st century. Science 1999; 284: 1311-1313.
6. Park Y, Lee DG, Jang SH, Woo ER, Jeong HG, Choi CH, Hahm KS. A Leu-Lys-rich antimicrobial peptide: activity and mechanism. Btochim. Biophys. Acta 2003; 1645: 172-182.
7. Machida S, Niimi S, Shi X, Ando Y, Yu Y. Design of a novel membrane-destabilizing peptide selectively acting on acidic liposomes. Biosci. Biotechnol. Biochem. 2000; 64: 985-994.
8. Blondelle SE, Houghten RA. Novel antimicrobial compounds identified using synthetic combinatorial library technology. Trends Biotechnol. 1996; 14: 60-65.
9. Hong SY, Oh JE, Kwon MY, Choi MJ, Lee JH, Lee BL, Moon HM, Lee KH. Identification and characterization of novel antimicrobial decapeptides generated by combinatorial chemistry. Antimicrob. Agents Chemother. 1998; 42: 2534-2541.
10. Whaley SR, English DS, Hu EL, Barbara PF, Belcher AM. Selection of peptides with semiconductor binding specificity for directed nanocrystal assembly. Nature 2000; 405: 665-668.
11. Zou W, Ueda M, Tanaka A. Screening of a molecule endowing Saccharomyces cerevisiae with n-nonane-tolerance from a combinatorial random protein library. Appl. Microbiol. Biotechnol. 2002; 58: 806-812.
12. Hanes J, Pluckthun A. In vitro selection and evolution of functional proteins by using ribosome display. Proc. Natl. Acad. Sci. U.S.A. 1997; 94: 4937-4942.
13. Zhou JM, Fujita S, Warashina M, Baba T, Taira K. A novel strategy by the action of ricin that connects phenotype and genotype without loss of the diversity of libraries. J. Am. Chem. Soc. 2002; 124: 538-543.
14. Cho G, Keefe AD, Liu R, Wilson DS, Szostak JW. Constructing high complexity synthetic libraries of long ORFs using in vitro selection. J. Mol. Biol. 2000; 297: 309-319.
15. Sidhu SS, Weiss GA, Wells JA. High copy display of large proteins on phage for functional selections. J. Mol. Biol. 2000; 296: 487-495.
16. Keefe AD, Szostak W. Functional proteins from a random-sequence library. Nature 2001; 410: 715-718.
17. Matsuzaki K, Murase O, Tokuda H, Funakoshi S, Fujii N, Miyajima K. Orientational and aggregational states of magainin 2 in phospholipid bilayers. Biochemistry 1994; 33: 3342-3349.
18. National Committee for Clinical Laboratory Standards. Methods for Dilution Antimicrobial Susceptibility Tests for Bacteria that Grow Aerobically (3rd edn). Approved standard NCCLS Documents M7-A3. The National Committee for Clinical Laboratory Standards: Wayne, Pennsylvania. USA, 1993.
19. Wieprecht T, Dathe M, Epand RM, Beyermann M, Krause E, Maloy WL, MacDonald DL, Bienert M. Influence of the angle subtended by the positively charged helix face on the membrane activity of amphipathic, antibacterial Peptides. Biochemistry 1997; 36: 12869-12880.
20. D-amino acid substitution and cyclization. J. Pept. Res. 2004; 64: 159-169.
21. 2 with model membrane systems and bacterial cells. J. Pept. Res. 2005; 65: 491-501.
22. dos Santos Cabrera MP, de Souza BM, Fontana R, Konno K, Palma MS, Azevero WF Jr, Neto JR. Conformation and lytic activity of eumenine mastoparan: a new antimicrobial peptide from wasp venom. J. Pept. Res. 2004; 64: 95-103.
23. Huang HW. Action of antimicrobial peptides: two-state model. Biochemistry 2000; 39: 8347-8352.
24. Park Y, Lee DG, Hahm KS. HP(2-9)-magainin 2(1-12), a synthetic hybrid peptide, exerts its antifungal effect on Candida albicans by damaging the plasma membrane. J. Pept. Sci. 2004; 10: 204-209.
25. Del Borgo MP, Hughes PA, Wade JD. Conformationally constrained single-chain peptide mimics of relaxin B chain secondary structure. J. Pept. Sci. 2005; 11: 564-571.
26. Sun X, Chen S, Li S, Yan H, Fan Y, Mi H. Deletion of two C-terminal Gln residues of 12-26-residue fragment of melittin improves its antimicrobial activity. Peptides 2005; 26: 369-375.
27. Giangaspero A, Sandri L, Tossi A. Amphipathic α-helical antimicrobial peptides. A systematic study of the effects of structural and physical properties on biological activity. Eur. J. Biochem. 2001; 268: 5589-5600.
28. Raventos D, Taboureau O, Mygind PH, Nielsen JD, Sonksen CP, Kristensen H-H. Improving on nature's defenses: optimization & high throughput screening of antimicrobial peptides. Comb. Chem. High Throughput Screen. 2005; 8: 219-233.
29. Taguchi S, Nakagawa K, Maeno M, Momose H. In vivo monitoring system for structure-function relationship analysis of the antimicrobial peptide apidaecin. Appl. Environ. Microbiol. 1994; 60: 3566-3572.
30. Rungpragayphan S, Nakano H, Yamane T. PCR-linked in vitro expression: a novel system for high throughput construction and screening of protein libraries. FEBS Lett. 2003; 540: 147-150.
31. Walker JR, Roth JR, Altman E. An in vivo study of novel bioactive peptides that inhibit the growth of Escherichia coli. J. Pept. Res. 2001; 58: 380-388.