Synthetic analogs of anoplin show improved antimicrobial activities

Journal of Peptide Science

Volumn 19, Issue 11, 2013, Pages 669-675

  Munk, Jens K ^a   Uggerhøj, Lars Erik ^b   Poulsen, Tanja J ^b   Frimodt Møller, Niels ^c   Wimmer, Reinhard ^b   Nyberg, Nils T ^a   Hansen, Paul R ^a  

^a UNIVERSITY OF COPENHAGEN   (Denmark)

^b AALBORG UNIVERSITY   (Denmark)

^c HVIDOVRE HOSPITAL   (Denmark)

Author keywords

Anoplin; Antimicrobial peptide; Antimicrobial resistance; Antimicrobials; Therapeutic index

Indexed keywords

2 NAPHTHYLALANINE; AMINO ACID; ANOPLIN DERIVATIVE; ANTIINFECTIVE AGENT; CYCLOHEXYLALANINE; GENTAMICIN; HEMOLYTIC AGENT; UNCLASSIFIED DRUG;

ANTIMICROBIAL ACTIVITY; ARTICLE; CONTROLLED STUDY; DRUG STRUCTURE; DRUG SYNTHESIS; ENTEROCOCCUS FAECIUM; ERYTHROCYTE; HEMOLYSIS; HUMAN; HYDROPHOBICITY; METHICILLIN RESISTANT STAPHYLOCOCCUS AUREUS; MINIMUM INHIBITORY CONCENTRATION; PRIORITY JOURNAL; PSEUDOMONAS AERUGINOSA; VANCOMYCIN RESISTANT ENTEROCOCCUS;

CANDIDA ALBICANS; ENTEROCOCCUS FAECIUM; ESCHERICHIA COLI; METHICILLIN RESISTANT STAPHYLOCOCCUS AUREUS; PSEUDOMONAS AERUGINOSA;

ANOPLIN; ANTIMICROBIAL PEPTIDE; ANTIMICROBIAL RESISTANCE; ANTIMICROBIALS; THERAPEUTIC INDEX;

ANTI-BACTERIAL AGENTS; ANTIFUNGAL AGENTS; ANTIMICROBIAL CATIONIC PEPTIDES; CANDIDA ALBICANS; DRUG RESISTANCE, BACTERIAL; ENTEROCOCCUS FAECIUM; ERYTHROCYTES; ESCHERICHIA COLI; HEMOLYTIC AGENTS; HUMANS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; METHICILLIN-RESISTANT STAPHYLOCOCCUS AUREUS; MICROBIAL SENSITIVITY TESTS; PSEUDOMONAS AERUGINOSA; WASP VENOMS;

EID: 84885940369     PISSN: 10752617     EISSN: 10991387     Source Type: Journal    
DOI: 10.1002/psc.2548     Document Type: Article

References (34)

1. Sharma A. Antimicrobial resistance: no action today, no cure tomorrow. Indian J. Med. Microbiol. 2011; 29: 91-2; DOI:10.4103/0255-0857.81774.
2. Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 2002; 415: 389-95; DOI:10.1038/415389a.
3. Fjell CD, Hiss JA, Hancock REW, Schneider G. Designing antimicrobial peptides: form follows function. Nat. Rev. Drug Discov. 2012; 11: 37-51; DOI:10.1038/nrd3591.
4. Pasupuleti M, Schmidtchen A, Malmsten M. Antimicrobial peptides: key components of the innate immune system. Crit. Rev. Biotechnol. 2012; 32: 143-71; DOI:10.3109/07388551.2011.594423.
5. Engler AC, Wiradharma N, Ong ZY, Coady DJ, Hedrick JL, Yang Y-Y. Emerging trends in macromolecular antimicrobials to fight multi-drug-resistant infections. Nano Today 2012; 7: 201-222; DOI:10.1016/j.nantod.2012.04.003.
6. Yeaman MR, Yount NY. Mechanisms of antimicrobial peptide action and resistance. Pharmacol. Rev. 2003; 55: 27-55; DOI:10.1124/pr.55.1.2.
7. Tossi A, Sandri L, Giangaspero A. Amphipathic, α-helical antimicrobial peptides. Biopolymers 2000; 55: 4-30; DOI:10.1002/1097-0282(2000)55:1<4::AID-BIP30>3.0.CO;2-M.
8. Dos Santos Cabrera MP, Arcisio-Miranda M, Broggio Costa ST, Konno K, Ruggiero JR, Procopio J, Ruggiero Neto J. Study of the mechanism of action of anoplin, a helical antimicrobial decapeptide with ion channel-like activity, and the role of the amidated C-terminus. J. Pept. Sci. 2008; 14: 661-9; DOI:10.1002/psc.960.
9. Xiong YQ, Yeaman MR, Bayer AS. In vitro antibacterial activities of platelet microbicidal protein and neutrophil defensin against Staphylococcus aureus are influenced by antibiotics differing in mechanism of action. Antimicrob Agents Chemother (Bethesda) 1999; 43: 1111-7.
10. Konno K, Hisada M, Fontana R, Lorenzi CCB, Naoki H, Itagaki Y, Miwa A, Kawai N, Nakata Y, Yasuhara T, Neto JR, De Azevedo Jr. WF, Palma MS, Nakajima T. Anoplin, a novel antimicrobial peptide from the venom of the solitary wasp Anoplius samariensis. Biochim. Biophys. Acta 2001; 1550: 70-80; DOI:10.1016/S0167-4838(01)00271-0.
11. Ifrah D, Doisy X, Ryge TS, Hansen PR. Structure-activity relationship study of anoplin. J. Pept. Sci. 2005; 11: 113-21; DOI:10.1002/psc.598.
12. Castano S, Cornut I, Büttner K, Dasseux JL, Dufourcq J. The amphipathic helix concept: length effects on ideally amphipathic LiKj(i=2j) peptides to acquire optimal hemolytic activity. B. B. A. (BBA) - Biomembr. 1999; 1416: 161-175; DOI:10.1016/S0005-2736(98)00219-3.
13. Slootweg JC, Van Schaik TB, Van Ufford HLCQ, Breukink E, Liskamp RMJ, Rijkers DTS. Improving the biological activity of the antimicrobial peptide anoplin by membrane anchoring through a lipophilic amino acid derivative. Bioorg. Med. Chem. Lett. 2013; 8-11; DOI:10.1016/j.bmcl.2013.05.002.
14. Pripotnev S, Won A, Ianoul A. The effects of l- to d-isomerization and C-terminus deamidation on the secondary structure of antimicrobial peptide anoplin in aqueous and membrane mimicking environment. J Raman Spectrosc 2010; 41: 1645-1649; DOI:10.1002/jrs.2608.
15. Won A, Khan M, Gustin S, Akpawu A, Seebun D, Avis TJ, Leung BO, Hitchcock AP, Ianoul A. Investigating the effects of l- to d-amino acid substitution and deamidation on the activity and membrane interactions of antimicrobial peptide anoplin. Biochim. Biophys. Acta 2011; 1808: 1592-600; DOI:10.1016/j.bbamem.2010.11.010.
16. Poulsen MH, Lucas S, Bach TB, Barslund AF, Wenzler C, Jensen CB, Kristensen AS, Strømgaard K. Structure-activity relationship studies of argiotoxins: selective and potent inhibitors of ionotropic glutamate receptors. J. Med. Chem. 2013; 56: 1171-81; DOI:10.1021/jm301602d.
17. Holzgrabe U. Quantitative NMR spectroscopy in pharmaceutical applications. Prog. Nucl. Magn. Reson. Spectrosc. 2010; 57: 229-40; DOI:10.1016/j.pnmrs.2010.05.001.
18. Wider G, Dreier L. Measuring protein concentrations by NMR spectroscopy. J. Am. Chem. Soc. 2006; 128: 2571-6; DOI:10.1021/ja055336t.
19. Mygind PH, Fischer RL, Schnorr KM, Hansen MT, Sönksen CP, Ludvigsen S, Raventós D, Buskov S, Christensen B, De Maria L, Taboureau O, Yaver D, Elvig-Jørgensen SG, Sørensen M, Christensen BE, Kjærulff S, Frimodt-Møller N, Lehrer RI, Zasloff M, et al. Plectasin is a peptide antibiotic with therapeutic potential from a saprophytic fungus. Nature 2005; 437: 975-80; DOI:10.1038/nature04051.
20. Mercier R-C, Stumpo C, Rybak MJ. Effect of growth phase and pH on the in vitro activity of a new glycopeptide, oritavancin (LY333328), against Staphylococcus aureus and Enterococcus faecium. J. Antimicrob. Chemother. 2002; 50: 19-24; DOI:10.1093/jac/dkf058.
21. Braun P, Von Heijne G. The aromatic residues Trp and Phe have different effects on the positioning of a transmembrane helix in the microsomal membrane. Biochemistry 1999; 38: 9778-82; DOI:10.1021/bi990923a.
22. Staubitz P, Peschel A, Nieuwenhuizen WF, Otto M, Götz F, Jung G, Jack RW. Structure-function relationships in the tryptophan-rich, antimicrobial peptide indolicidin. J. Pept. Sci. 2001; 7: 552-64; DOI:10.1002/psc.351.
23. Ryge TS, Doisy X, Ifrah D, Olsen JE, Hansen PR. New indolicidin analogues with potent antibacterial activity. J. Pept. Res. 2004; 64: 171-85; DOI:10.1111/j.1399-3011.2004.00177.x.
24. Glukhov E, Stark M, Burrows LL, Deber CM. Basis for selectivity of cationic antimicrobial peptides for bacterial versus mammalian membranes. J. Biol. Chem. 2005; 280: 33960-7; DOI:10.1074/jbc.M507042200.
25. Wiradharma N, Khoe U, Hauser CAE, Seow SV, Zhang S, Yang Y-Y. Synthetic cationic amphiphilic α-helical peptides as antimicrobial agents. Biomaterials 2011; 32: 2204-12; DOI:10.1016/j.biomaterials.2010.11.054.
26. Chen Y, Mant CT, Farmer SW, Hancock REW, Vasil ML, Hodges RS. Rational design of α-helical antimicrobial peptides with enhanced activities and specificity/therapeutic index. J. Biol. Chem. 2005; 280: 12316-29; DOI:10.1074/jbc.M413406200.
27. Schmitt MA, Weisblum B, Gellman SH. Interplay among folding, sequence, and lipophilicity in the antibacterial and hemolytic activities of α/β-peptides. J. Am. Chem. Soc. 2007; 129: 417-28; DOI:10.1021/ja0666553.
28. Yang N, Lejon T, Rekdal O. Antitumour activity and specificity as a function of substitutions in the lipophilic sector of helical lactoferrin-derived peptide. J. Pept. Sci. 2003; 9: 300-11; DOI:10.1002/psc.457.
29. Epand RM, Epand RF. Lipid domains in bacterial membranes and the action of antimicrobial agents. B. B. A. 2009; 1788: 289-94.
30. Mileykovskaya E, Dowhan W. Cardiolipin membrane domains in prokaryotes and eukaryotes. Biochim. Biophys. Acta 2009; 1788: 2084-91; DOI:10.1016/j.bbamem.2009.04.003.
31. Mishra NN, Bayer AS, Tran TT, Shamoo Y, Mileykovskaya E, Dowhan W, Guan Z, Arias CA. Daptomycin resistance in enterococci is associated with distinct alterations of cell membrane phospholipid content. PLoS One 2012; 7: e43958; DOI:10.1371/journal.pone.0043958.
32. Wessolowski A, Bienert M, Dathe M. Antimicrobial activity of arginine- and tryptophan-rich hexapeptides: the effects of aromatic clusters, d-amino acid substitution and cyclization. J. Pept. Res. 2004; 64: 159-69; DOI:10.1111/j.1399-3011.2004.00182.x.
33. Dathe M, Nikolenko H, Klose J, Bienert M. Cyclization increases the antimicrobial activity and selectivity of arginine- and tryptophan-containing hexapeptides. Biochemistry 2004; 43: 9140-50; DOI:10.1021/bi035948v.
34. Hensler ME, Bernstein G, Nizet V, Nefzi A. Pyrrolidine bis-cyclic guanidines with antimicrobial activity against drug-resistant Gram-positive pathogens identified from a mixture-based combinatorial library. Bioorg. Med. Chem. Lett. 2006; 16: 5073-9; DOI:10.1016/j.bmcl.2006.07.037.