Antibacterial activity of poly-l-arginine under different conditions
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Abstract
Background and Objectives: Arginine-rich peptides are an important class of antimicrobial peptides (AMPs) that exert their antibacterial activity via a lytic mechanism. Although the antibacterial activity of arginine-rich peptides has been already evaluated, no reports have so far been evaluated the influence of reaction conditions on their antimicrobial potential. The aim of the present study was to investigate the influence of pH, temperature, and glycine on antibacterial activity of poly-l-arginine (PLA) with a molecular weight of 5-15 kDa against Escherichia coli O157:H7 and Staphylococcus aureus.
Materials and Methods: The percentage of growth inhibition of PLA against both bacteria was analyzed at various pH, temperatures and sub-inhibitory concentrations of glycine by two-fold broth microdilution method.
Results: The results showed that PLA had antibacterial activity against E. coli O157:H7 and S. aureus and the inhibitory effect increased with increasing PLA concentration. The antimicrobial activity of PLA against both microorganisms was higher in basic media than under acidic or neutral conditions. At 1/2 times the MIC, heat treatment intensified the toxicity of PLA against E. coli O157:H7 whereas the susceptibility to PLA seems to be temperature independent for S. aureus. The MICs of glycine against E. coli O157:H7 and S. aureus were 12.5 and 25 mg ml-1, respectively. The antibacterial activity of PLA against both microorganisms increased, as indicated by the increasing growth inhibition percentage of this peptide with increasing glycine concentration.
Conclusion: The antibacterial activity of PLA against S. aureus and E. coli O157:H7 depends on pH and glycine concentration.
Parish ME, Beuchat LR, Suslow TV, Harris LJ, Garrett EH, Farber JN, et al. Methods to reduce/eliminate pathogens from fresh and fresh-cut produce. Compr Rev Food Sci Food Saf 2003; 2: 161-173.
Costanza F, Padhee S, Wu H, Wang Y, Revenis J, Cao C, et al. Investigation of antimicrobial PEG-poly(amino acid)s. RSC Adv 2014; 4: 2089-2095.
Szókán G, Almas M, Krizsan K, Khlafulla AR, Tyihak E. Structure determination and synthesis of lysine isopeptides influencing on cell proliferation. Biopolymers 1997; 42: 305-318.
Li YQ, Han Q, Feng JL, Tian WL, Mo HZ. Antibacterial characteristics and mechanisms of ɛ-poly-lysine against Escherichia coli and Staphylococcus aureus. Food Control 2014; 43: 22-27.
Plianwong S, Opanasopit P, Ngawhirunpat T, Rojanarata T. Chitosan combined with poly-L-arginine as efficient, safe, and serum-insensitive vehicle with RNase protection ability for siRNA delivery. Biomed Res Int 2013;2013:574136.
Yamaki T, Uchida M, Kuwahara Y, Shimazaki Y, Ohtake K, Kimura M, et al. Effect of poly-L-arginine on intestinal absorption of hydrophilic macromolecules in rats. Biol Pharm. Bull 2013; 36: 496-500.
Vidal L, Thuault V, Mangas A, Coveñas R, Thienpont A, Geffard M. Lauryl-poly-L-lysine: A new antimicrobial agent?. J Amino Acids 2014;2014:672367.
Nishikawa M, Ogawa KI. Antimicrobial activity of a chelatable poly (arginyl-histidine) produced by the ergot fungus Verticillium kibiense. Antimicrob Agents Chemother 2004; 48: 229-235.
Böger RH. The pharmacodynamics of L-arginine. J Nutr 2007; 137: 1650S-1655S.
Meloni BP, Brookes LM, Clark VW, Cross JL, Edwards AB, Anderton RS, et al. Poly-arginine and arginine-rich peptides are neuroprotective in stroke models. J Cereb Blood Flow Metab 2015; 35: 993-1004.
Li L, Vorobyov I, Allen TW. The different interactions of lysine and arginine side chains with lipid membranes. J Phys Chem B 2013; 117: 11906-11920.
Nemoto E, Takahashi H, Kobayashi D, Ueda H, Morimoto Y. Effects of poly-L-arginine on the permeation of hydrophilic compounds through surface ocular tissues. Biol Pharm Bull 2006; 29: 155-160.
Westergren I, Johnansson BB. Altering the blood-brain barrier in the rat by intracarotid infusion of polycations: a comparison between protamine, poly-L-lysine and poly-L-arginine. Acta Physiol Scand 1993; 149: 99-104.
Lan Q, Wang Y, Wang S, Liu Y. In vitro study of alginate/poly-L-arginine microcapsules as a protein or anticancer drug carrier. IFMBE Proceedings 2008; 19: 32-35.
Mattner F, Fleitmann JK, Lingnau K, Schmidt W, Egyed A, Fritz J, et al. Vaccination with Poly-l-Arginine As Immunostimulant for Peptide Vaccines: Induction of Potent and Long-Lasting T-Cell Responses against Cancer Antigens. Cancer Res 2002; 62: 1477-1480.
Kim EJ, Shim G, Kim K, Kwon IC, Oh YK, Shim CK. Hyaluronic acid complexed to biodegradable poly-L-arginine for targeted delivery of siRNAs. J Gene Med 2009; 11: 791-803.
Elżbieciak-Wodka M, Warszyński P. Effect of deposition conditions on thickness and permeability of the multilayer films formed from natural polyelectrolytes. Electrochimica Acta 2013; 104: 348-357.
Holo H, Nes IF. High-frequency transformation, by electroporation, of Lactococcus lactis subsp. cremoris grown with glycine in osmotically stabilized media. Appl Environ Microbiol 1989; 55: 3119-3123.
Minami M, Ando T, Hashikawa SN, Torii K, Hasegawa T, Israel DA, et al. Effect of glycine on Helicobacter pylori in vitro. Antimicrob Agents Chemother 2004; 48: 3782-3788.
Izadpanah A, Gallo RL. Antimicrobial peptides. J Am Acad Dermatol 2005; 52: 381-390.
Rezansoff AJ, Hunter HN, Jing W, Park IY, Kim SC. Interactions of the antimicrobial peptide Ac-FRWWHR-NH2 with model membrane systems and bacterial cells. J Pept Res 2005; 65: 491-501.
Subbalakshmi C, Sitaram N. Mechanism of antimicrobial action of indolicidin. FEMS Microbiol Lett 1998; 160: 91-96.
Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 2002; 415: 389-395.
Conte M, Aliberti F, Fucci L, Piscopo M. Antimicrobial activity of various cationic molecules on foodborne pathogens. World J Microbiol Biotechnol 2007; 23: 1679-1683.
Beveridge TJ. Structures of gram-negative cell walls and their derived membrane vesicles. J bacterial 1999; 181: 4725-4733.
Walkenhorst WF, Klein JW, Vo P, Wimley WC. pH dependence of microbe sterilization by cationic antimicrobial peptides. Antimicrob Agents Chemother 2013; 57: 3312-3320.
Mackay BJ, Denepitiya L, Iacono VJ, Krost SB, Pollock JJ. Growth-inhibitory and bactericidal effects of human parotid salivary histidine-rich polypeptides on Streptococcus mutans. Infect Immun 1984; 44: 695-701.
Swoboda JG, Campbell J, Meredith TC, Walker S. Wall teichoic acid function, biosynthesis, and inhibition. Chembiochem 2010; 11: 35-45.
Weidenmaier C, Peschel A. Teichoic acids and related cell-wall glycopolymers in Gram-positive physiology and host interactions. Nat Rev Microbiol 2008; 6: 276-287.
Neuhaus FC, Baddiley J. A continuum of Anionix Charge: structures and functions of D-alanyl-teichoic acids in gram-positive bacteria. Microbiol Mol Biol Rev 2003; 67: 686-723.
Bernal P, Zloh M, Taylor PW. Disruption of D-alanyl esterification of Staphylococcus aureus cell wall teichoic acid by the β-lactam resistance modifier (–)-epicatechin gallate. J Antimicrob Chemother 2009; 63: 1156-1162.
Kim SH, Jia W, Parreira VR, Bishop RE, Gyles, CL. Phosphoethanolamine substitution in the lipid A of Escherichia coli O157: H7 and its association with PmrC. Microbiology 2006; 152: 657-666.
Raetz CR, Reynolds CM, Trent MS, Bishop RE. Lipid A modification systems in gram-negative bacteria. Annu Rev Biochem 2007; 76: 295-329.
Gunn JS, Ryan SS, Van Velkinburgh JC, Ernst RK, Miller SI. Genetic and functional analysis of a PmrA-PmrB-regulated locus necessary for lipopolysaccharide modification, antimicrobial peptide resistance, and oral virulence of Salmonella enterica Serovar Typhimurium. Infect Immun 2000; 68: 6139-6146.
Lee H, Hsu FF, Turk J, Groisman EA. The PmrA-regulated pmrC gene mediates phosphoethanolamine modification of lipid A and polymyxin resistance in Salmonella enterica. J Bacteriol 2004; 186: 4124-4133.
Reinés M, Llobet E, Llompart CM, Moranta D, Pérez-Gutiérrez C, Bengoechea JA. Molecular basis of Yersinia enterocolitica temperature-dependent resistance to antimicrobial peptides. J Bacteriol 2012; 194: 3173-3188.
Charles AS, Baskaran SA, Murcott C, Schreiber D, Hoagland T, Venkitanarayanan K. Reduction of Escherichia coli O157: H7 in cattle drinking-water by trans-cinnamaldehyde. Foodborne Pathog Dis 2008; 5: 763-771.
McElhaney RN, Souza KA. The relationship between environmental temperature, cell growth and the fluidity and physical state of the membrane lipids in Bacillus stearothermophilus. Biochim Biophys Acta 1976; 443: 348-359.
Martinsen B, Oppegaard H, Wichstrøm R, Myhr E. Temperature-dependent in vitro antimicrobial activity of four 4-quinolones and oxytetracycline against bacteria pathogenic to fish. Antimicrob Agents Chemother 1992; 36: 1738-1743.
Jabasingh SA, Nachiyar CV. Utilization of pretreated bagasse for the sustainable bioproduction of cellulae by Aspergillus nidulans MTCC344 using response surface methodology. Ind Crop Prod 2011; 34: 1564-1571.
Schwartz AC, Quecke W, Brenschede G. Inhibition by glycine of the catabolic reduction of proline in Clostridium sticklandii: evidence on the regulation of amino acid reduction. Z Allg Mikrobiol 1979; 19: 211-220.
Gillissen G, Schumacher M, Breuer-Werle M. Modulation of antimicrobial effects of beta-lactams by amino acids in vitro. Zentralbl Bakteriol 1991; 275: 223-232.
Hammes W, Schleifer KH, Kandler O. Mode of action of glycine on the biosynthesis of peptidoglycan. J Bacteriol 1973; 116: 1029-1053.
Hishinuma F, Izaki K, Takahashi H. Effects of glycine and D-amino acids on growth of various microorganisms. Agric Biol Chem 1969; 33: 1577-1586.
Cosquer A, Ficamos M, Jebbar M, Corbel JC, Choquet G, Fontenelle C, et al. Antibacterial activity of glycine betaine analogues: involvement of osmoporters. Bioorg Med Chem Lett 2004; 14: 2061-2065.
Stănilă A, Braicu C, Stănilă S, Pop RM. Antibacterial activity of copper and cobalt amino acids complexes. Not Bot Horti Agrobot 2011; 39(2): 124-129.
Al-Maythalony BA, Monim-ul-Mehboob M, Wazeer MI, Isab AA, Shaikh MN, Altuwaijri S. Synthesis, CP-MAS NMR characterization, and antibacterial activities of glycine and histidine complexes of Cd (SeCN)2 and Hg (SeCN)2. Bioinorg Chem Appl 2013; doi: 10.1155/2013/476874.
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| Issue | Vol 9 No 2 (2017) | |
| Section | Original Article(s) | |
| Keywords | ||
| Antibacterial activity Escherichia coli O157 H7 Glycine Poly-l-arginine Staphylococcus aureus | ||
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