Functional gold nanoparticle-based antibacterial agents for nosocomial and antibiotic-resistant bacteria

Nanomedicine

Volumn 11, Issue 19, 2016, Pages 2497-2510

  Kuo, Yen Ling ^a   Wang, Sin Ge ^a   Wu, Ching Yi ^a   Lee, Kai Chieh ^a   Jao, Chan Jung ^a   Chou, Shiu Huey ^b   Chen, Yu Chie ^a  

^a NATIONAL CHIAO TUNG UNIVERSITY   (Taiwan)

^b FU JEN CATHOLIC UNIVERSITY   (Taiwan)

Author keywords

antibacterial peptides; antibiotic resistant bacteria; antibiotics; Au NPs; Enterococcus faecalis; Enterococcus faecium; macrophages; MRSA; Staphylococcus aureus; VRE

Indexed keywords

ANTIINFECTIVE AGENT; ARGININE; CYSTEINE; GOLD NANOPARTICLE; TRYPTOPHAN; GOLD; METAL NANOPARTICLE; OLIGOPEPTIDE;

ABSORPTION SPECTROSCOPY; ANTIBIOTIC RESISTANCE; ARTICLE; BACTERIAL INFECTION; BACTERIAL MEMBRANE; BACTERIAL STRAIN; BINDING AFFINITY; CELL GROWTH; CONTROLLED STUDY; ENTEROCOCCUS FAECALIS; ENTEROCOCCUS FAECIUM; ENTOMOPATHOGENIC BACTERIUM; ESCHERICHIA COLI O157; HEMOLYSIS ASSAY; HOSPITAL INFECTION; KLEBSIELLA PNEUMONIAE; MACROPHAGE; METHICILLIN RESISTANT STAPHYLOCOCCUS AUREUS; MOUSE; NANOTECHNOLOGY; NONHUMAN; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; PROTEIN BINDING; STAPHYLOCOCCUS; ANIMAL; CHEMISTRY; CROSS INFECTION; DRUG EFFECTS; ENTEROCOCCUS; ESCHERICHIA COLI; HUMAN; MICROBIAL SENSITIVITY TEST; MICROBIOLOGY; PARTICLE SIZE; RAW 264.7 CELL LINE; SURFACE PROPERTY;

ANIMALS; ANTI-BACTERIAL AGENTS; ARGININE; BACTERIAL INFECTIONS; CROSS INFECTION; DRUG RESISTANCE, BACTERIAL; ENTEROCOCCUS; ESCHERICHIA COLI; GOLD; HUMANS; MACROPHAGES; METAL NANOPARTICLES; MICE; MICROBIAL SENSITIVITY TESTS; OLIGOPEPTIDES; PARTICLE SIZE; RAW 264.7 CELLS; STAPHYLOCOCCUS; SURFACE PROPERTIES; TRYPTOPHAN;

EID: 84990243540     PISSN: 17435889     EISSN: 17486963     Source Type: Journal    
DOI: 10.2217/nnm-2016-0232     Document Type: Article

References (56)

1. Walsh CT, Wencewicz TA. Prospects for new antibiotics: a molecule-centered perspective. J. Antibiot. 67, 7-22 (2014).
2. Rayamajhi N, Cha SB, Yoo HS. Antibiotics resistances: past, present and future. J. Biomed. Res. 11, 65-80 (2010).
3. Hancock RE, Chapple DS. Peptide antibiotics. Antimicrob. Agents Chemother. 43, 1317-1323 (1999).
4. Odell EW, Sarra R, Foxworthy M, Chapple DS, Evans RW. Antibacterial activity of peptides homologous to a loop region in human lactoferrin. FEBS Lett. 382, 175-178 (1996).
5. Ganz T, Lehrer RI. Antimicrobial peptides of leukocytes. Curr. Opin. Hematol. 4, 53-58 (1997).
6. Zasloff M. A class of antimicrobial peptides from xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor. Proc. Natl Acad. Sci. USA 84, 5449-5453 (1987).
7. Csordas A, Michl H. Isolation and structure of a haemolytic polypeptide from the defensive secretion of European Bombina species. Monatsh. Chem. 101, 182-189 (1970).
8. Habermann E. Bee and wasp venoms Science 177, 314-322 (1972).
9. Hultmark D, Steiner H, Rasmuson T, Boman HG. Insect immunity. Purification and properties of three inducible bactericidal proteins from hemolymph of immunized pupae of hyalophora cecropia. Eur. J. Biochem. 106, 7-16 (1980).
10. García Olmedo F, Molina Fernández A, Alamillo JM, Rodriguez Palenzuela P. Plant defense peptides. Biopolymers 47, 479-491 (1998).
11. Jack RW, Jung G. Natural peptides with antimicrobial activity. Chimia 52, 48-55 (1998).
12. Baba T, Schneewind O. Instruments of microbial warfare: bacteriocin synthesis, toxicity and immunity. Trends Microbiol. 6, 66-71 (1998).
13. Abee T. Pore-forming bacteriocins of gram-positive bacteria and self-protection mechanisms of producer organisms. FEMS Microbiol. Lett. 129, 1-9 (1995).
14. Tencza SB, Douglass JP, Creighton D, Montelaro RC, Mietzner TA. Novel antimicrobial peptides derived from human immunodeficiency virus type 1 and other lentivirus transmembrane proteins. Antimicrob. Agents Chemother. 41, 2394-2398 (1997).
15. Eisenberg D, Wesson M. The most highly amphiphilic alpha-helices include two amino acid segments in human immunodeficiency virus glycoprotein. Biopolymers 29, 171-177 (1990).
16. Hancock RE. Peptide antibiotics. Lancet 349, 418-422 (1997).
17. Ibrahim HR, Thomas U, Pellegrini A. A helix-loop-helix peptide at the upper lip of the active site cleft of lysozyme confers potent antimicrobial activity with membrane permeabilization action. J. Biol. Chem. 276, 43767-43774 (2001).
18. Chapple DS, Hussain R, Joannou CL et al. Structure and association of human lactoferrin peptides with Escherichia coli lipopolysaccharide. Antimicrob. Agents Chemother. 48, 2190-2198 (2004).
19. Lupetti A, Paulusma-Annema A, Welling MM, Senesi S, van Dissel JT, Nibbering PH. Candidacidal activities of human lactoferrin peptides derived from the N terminus. Antimicrob. Agents Chemother. 44, 3257-3263 (2000).
20. Wakabayashi H, Takase M, Tomita M. Lactoferricin derived from milk protein lactoferrin. Curr. Pharm. Des. 9, 1277-1287 (2003).
21. Vorland LH, Ulvatne H, Andersen J, Haukland HH, Rekdal O, Svendsen JS, Gutteberg TJ. Lactoferricin of bovine origin is more active than lactoferricins of human, murine and caprine origin. Scand. J. Infect. Dis. 30, 513-517 (1998).
22. Bellamy W, Takase M, Wakabayashi H, Kawase K, Tomita M. Antibacterial spectrum of lactoferricin B, A potent bactericidal peptide derived from the N-terminal region of bovine lactoferrin. J. Appl. Bacteriol. 73, 472-479 (1992).
23. Pellegrini A, Thomas U, Bramaz N, Klauser S, Hunziker P, Von Fellenberg R. Identification and isolation of a bactericidal domain in chicken egg white lysozyme. J. Appl. Microbiol. 82, 372-378 (1997).
24. Blondelle SE, Houghten RA. Novel antimicrobial compounds identified using synthetic combinatorial library technology. Trends Biotechnol. 14, 60-65 (1996).
25. Capparelli R, Amoroso MG, Palumbo D, Iannaccone M, Faleri C, Cresti M. Two plant puroindolines colocalize in wheat seed and in vitro synergistically fight against pathogens. Plant Mol. Biol. 58, 857-867 (2005).
26. Jing W, Demcoe AR, Vogel HJ. Conformation of a bactericidal domain of puroindoline a: structure and mechanism of action of a 13-residue antimicrobial peptide. J. Bacteriol. 185, 4938-4947 (2003).
27. Falla TJ, Karunaratne DN, Hancock RE. Mode of action of the antimicrobial peptide indolicidin. J. Biol. Chem. 271, 19298-19303 (1996).
28. Yang ST, Shin SY, Kim YC, Kim Y, Hahm KS, Kim JI. Conformation-dependent antibiotic activity of tritrpticin, a cathelicidin-derived antimicrobial peptide. Biochem. Biophys. Res. Commun. 296, 1044-1050 (2002).
29. Clark DP, Durell S, Maloy WL, Zaslof M. Ranalexin. A novel antimicrobial peptide from bullfrog (Rana catesbeiana) skin, structurally related to the bacterial antibiotic, polymyxin. J. Biol. Chem. 269, 10849-10855 (1994).
30. Selsted ME, Novotnytll MJ, Morris WL, Tang Y, Smith W, Cullor JS. Indolicidin, a novel bactericidal tridecapeptide amide from neutrophils. J. Biol. Chem. 267, 4292-4295 (1992).
31. Friedrich CL, Rozek A, Patrzykat A, Hancock RE. Structure and mechanism of action of an indolicidin peptide derivative with improved activity against Gram-positive bacteria. J. Biol. Chem. 276, 24015-24022 (2001).
32. Schibli DJ, Hwang PM, Vogel HJ. Structure of the antimicrobial peptide tritrpticin bound to micelles: a distinct membrane-bound peptide fold. Biochemistry 38, 16749-16755 (1999).
33. Wei SY, Wu JM, Kuo YY et al. Solution structure of a novel tryptophan-rich peptide with bidirectional antimicrobial activity. J. Bacteriol. 188, 328-334 (2006).
34. Chan DI, Prenner EJ, Vogel HJ. Tryptophan-and argininerich antimicrobial peptides: structures and mechanisms of action. Biochim Biophys. Acta. 1758, 1184-1202 (2006).
35. Hancock RE, Sahl HG. Antimicrobial and host-defense peptides as new anti-infective therapeutic strategies. Nat. Biotechnol. 24, 1551-1557 (2006).
36. Hancock RE. Cationic peptides: effectors in innate immunity and novel antimicrobials. Lancet. Infect. Dis. 1, 156-164 (2001).
37. Chan P-H, Chen Y-C. Human serum albumin stabilized gold nanoclusters as selective luminescent probes for staphylococcus aureus and Methicillin-resistant Staphylococcus aureus. Anal. Chem. 84, 8952-8956 (2012).
38. Lai H-Z, Wang SG, Wu CY, Chen Y-C. Detection of Staphylococcus aureus by functional gold nanoparticle-based affinity surface-assisted laser desorption/ionization mass spectrometry. Anal. Chem. 87, 2114-2120 (2015).
39. Gu HW, Ho PL, Tong E, Wang L, Xu B. Presenting vancomycin on nanoparticles to enhance antimicrobial activities. Nano Lett. 3, 1261-1263 (2003).
40. Shahverdi AR, Fakhimi A, Shahverdi HR, Minaian S. Synthesis and effect of silver nanoparticles on the antibacterial activity of different antibiotics against Staphylococcus aureus and Escherichia coli. Nanomedicine 3, 168-171 (2007).
41. Huang W-C, Tsai P-J, Chen Y-C. Functional gold nanoparticles as photothermal agents for selective-killing of pathogenic bacteria. Nanomedicine 2, 777-787 (2007).
42. Eby DM, Farrington KE, Johnson GR. Synthesis of bioinorganic antimicrobial peptide nanoparticles with potential therapeutic properties. Biomacromolecules 9, 2487-2494 (2008).
43. Huang W-C, Tsai P-J, Chen Y-C. Multifunctional Fe3O4@ Au nanoeggs as photothermal agents for selective killing of nosocomial and antibiotic-resistant bacteria. Small 5, 51-56 (2009).
44. Lai H-Z, Chen W-Y, Wu C-Y, Chen Y-C. Potent antibacterial nanoparticles for pathogenic bacteria. ACS Appl. Mater. Inter. 7, 2046-2054 (2015).
45. Chen W-J, Chen Y-C. Fe3O4/TiO2 core/shell magnetic nanoparticle-based photokilling of pathogenic bacteria. Nanomedicine 5, 1585-1593 (2010).
46. Mohanty S, Jena P, Mehta R et al. Cationic antimicrobial peptides and biogenic silver nanoparticles kill mycobacteria without eliciting DNA damage and cytotoxicity in mouse macrophages. Antimicrob Agents Chemother. 57, 3688-3698 (2013).
47. Chen W-Y, Chang H-Y, Lu J-K et al. Self-assembly of antimicrobial peptides on gold nanodots: against multidrugresistant bacteria and wound-healing application. Adv. Funct. Mater. 25, 7189-7199 (2015).
48. Water JJ, Smart S, Franzyk H, Foged C, Nielsen HM. Nanoparticle-mediated delivery of the antimicrobial peptide plectasin against Staphylococcus aureus in infected epithelial cells. Eur. J. Pharm. Biopharm. 92, 65-73 (2015).
49. Beyth N, Houri-Haddad Y, Domb A, Khan W, Hazan R. Alternative antimicrobial approach: nano-antimicrobial materials. Evid. Based. Complement Alternat Med. 2015, 246012 (2015).
50. Selvaprakash K, Chen Y-C. Using protein-encapsulated gold nanoclusters as photoluminescent sensing probes for biomolecules. Biosens. Bioelectron. 61, 88-94 (2014).
51. Chan P-H, Ghosh B, Lai H-Z, Peng H-L, Mong K-KT, Chen Y-C. Photoluminescent gold nanoclusters as sensing probes for uropathogenic Escherichia coli. PLoS ONE 8, e58064 (2013).
52. Zhou TY, Lin LP, Rong MC, Jiang YQ, Chen X. Silvergold alloy nanoclusters as a fluorescence-enhanced probe for aluminum ion sensing. Anal. Chem. 85, 9839-9844 (2013).
53. Bourg MC, Badia A, Lennox RB. Gold-sulfur bonding in 2D and 3D self-assembled monolayers: XPS characterization. J. Phys. Chem. B 104, 6562-6567 (2000).
54. Kubica M, Guzik K, Koziel J et al. A potential new pathway for Staphylococcus aureus dissemination: the silent survival of S. aureus phagocytosed by human monocyte-derived macrophages. PLoS ONE 3, e1409 (2008).
55. Xia Z, Triffitt JT. A review on macrophage responses to biomaterials. Biomed. Mater. 1, R1-R9 (2006).
56. Sakamoto K, Margolles A, Van Veen HW, Konings WN. Hop resistance in the beer spoilage bacterium Lactobacillus brevis is mediated by the ATP-binding cassette multidrug transporter HorA. J. Bacteriol. 183, 5371-5375 (2001).