Abstract
Biofilms are the major concerns to the researchers, due to their universal distribution among prokaryotes and involvement in antibiotic drug resistance towards conventional drugs. It led the bacteria to become up to 1000 times resistant towards antibiotics. Therefore, diverse types of anti-biofilm agents are continuously designed to target them namely (phyto) chemicals, peptides, enzymes, biosurfactants, microbial extracts, nanoparticles, and many more. Antibiofilm peptides have demonstrated high potential in targeting biofilm due to their low toxicity, and off-target effects. These peptides are experimentally validated to disrupt most of the biofilms developed on medical devices like catheters, stents, dentures, etc. implicated in nosocomial infections by ESKAPE pathogens. However, one of the important reasons for the peptides, to emerge as a new hope against biofilms, is their wide mode of action against different stages and microbial species. In the present chapter, we are focusing to explore various aspects of this important class of antibiofilm therapeutics.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Agarwala M, Choudhury B, Yadav RN (2014) Comparative study of antibiofilm activity of copper oxide and iron oxide nanoparticles against multidrug resistant biofilm forming uropathogens. Ind J Microbiol 54:365–368. https://doi.org/10.1007/s12088-014-0462-z
Ahiwale SS, Bankar AV, Tagunde S, Kapadnis BP (2017) A bacteriophage mediated gold nanoparticles synthesis and their anti-biofilm activity. Ind J Microbiol 57:188–194. https://doi.org/10.1007/s12088-017-0640-x
Anunthawan T, de la Fuente-Nunez C, Hancock RE, Klaynongsruang S (2015) Cationic amphipathic peptides KT2 and RT2 are taken up into bacterial cells and kill planktonic and biofilm bacteria. Biochim Biophys Acta 1848:1352–1358. https://doi.org/10.1016/j.bbamem.2015.02.021
Balamurugan P, Hema M, Kaur G, Sridharan V, Prabu PC, Sumana MN, Princy SA (2015) Development of a biofilm inhibitor molecule against multidrug resistant Staphylococcus aureus associated with gestational urinary tract infections. Front Microbiol 6:832. https://doi.org/10.3389/fmicb.2015.00832
Batoni G, Maisetta G, Esin S (2016) Antimicrobial peptides and their interaction with biofilms of medically relevant bacteria. Biochim Biophys Acta 1858:1044–1060. https://doi.org/10.1016/j.bbamem.2015.10.013
Bhargava N, Singh SP, Sharma A, Sharma P, Capalash N (2015) Attenuation of quorum sensing-mediated virulence of Acinetobacter baumannii by Glycyrrhiza glabra flavonoids. Future Microbiol 10:1953–1968. https://doi.org/10.2217/fmb.15.107
Blower RJ, Barksdale SM, van Hoek ML (2015) Snake Cathelicidin NA-CATH and Smaller Helical Antimicrobial Peptides Are Effective against Burkholderia thailandensis. PLoS Negl Trop Dis 9: e0003862. doi:https://doi.org/10.1371/journal.pntd.0003862
Brancatisano FL, Maisetta G, Di Luca M, Esin S, Bottai D, Bizzarri R, Campa M, Batoni G (2014) Inhibitory effect of the human liver-derived antimicrobial peptide hepcidin 20 on biofilms of polysaccharide intercellular adhesin (PIA)-positive and PIA-negative strains of Staphylococcus epidermidis. Biofouling 30:435–446. https://doi.org/10.1080/08927014.2014.888062
Branda SS, Vik S, Friedman L, Kolter R (2005) Biofilms: the matrix revisited. Trends Microbiol 13:20–26. https://doi.org/10.1016/j.tim.2004.11.006
Cardoso MH, Ribeiro SM, Nolasco DO, de la Fuente-Nunez C, Felicio MR, Goncalves S, Matos CO, Liao LM, Santos NC, Hancock RE, Franco OL, Migliolo L (2016) A polyalanine peptide derived from polar fish with anti-infectious activities. Sci Rep 6: 21385. doi:https://doi.org/10.1038/srep21385
Choi H, Lee DG (2012) Antimicrobial peptide pleurocidin synergizes with antibiotics through hydroxyl radical formation and membrane damage, and exerts antibiofilm activity. Biochim Biophys Acta 1820:1831–1838. https://doi.org/10.1016/j.bbagen.2012.08.012
Conrad A, Suutari MK, Keinanen MM, Cadoret A, Faure P, Mansuy-Huault L, Block JC (2003) Fatty acids of lipid fractions in extracellular polymeric substances of activated sludge flocs. Lipids 38:1093–1105
Dang H, Lovell CR (2016) Microbial surface colonization and biofilm development in marine environments. Microbiol Mol Biol Rev 80:91–138. https://doi.org/10.1128/mmbr.00037-15
Davey ME, O’Toole GA (2000) Microbial biofilms: from ecology to molecular genetics. Microbiol Mol Biol Rev 64:847–867
Davey ME, Caiazza NC, O’Toole GA (2003) Rhamnolipid surfactant production affects biofilm architecture in Pseudomonas aeruginosa PAO1. J Bacteriol 185:1027–1036
de la Fuente-Nunez C, Korolik V, Bains M, Nguyen U, Breidenstein EB, Horsman S, Lewenza S, Burrows L, Hancock RE (2012) Inhibition of bacterial biofilm formation and swarming motility by a small synthetic cationic peptide. Antimicrob Agents Chemother 56:2696–2704. https://doi.org/10.1128/aac.00064-12
de la Fuente-Nunez C, Mansour SC, Wang Z, Jiang L, Breidenstein EB, Elliott M, Reffuveille F, Speert DP, Reckseidler-Zenteno SL, Shen Y, Haapasalo M, Hancock RE (2014) Anti-biofilm and immunomodulatory activities of peptides that inhibit biofilms formed by pathogens isolated from cystic fibrosis patients. Antibiotics (Basel) 3:509–526. https://doi.org/10.3390/antibiotics3040509
de la Fuente-Nunez C, Reffuveille F, Mansour SC, Reckseidler-Zenteno SL, Hernandez D, Brackman G, Coenye T, Hancock RE (2015) D-enantiomeric peptides that eradicate wild-type and multidrug-resistant biofilms and protect against lethal Pseudomonas aeruginosa infections. Chem Biol 22:196–205. https://doi.org/10.1016/j.chembiol.2015.01.002
de la Fuente-Nunez C, Cardoso MH, de Souza Candido E, Franco OL, Hancock RE (2016) Synthetic antibiofilm peptides. Biochim Biophys Acta 1858:1061–1069. https://doi.org/10.1016/j.bbamem.2015.12.015
Delattin N, De Brucker K, Craik DJ, Cheneval O, Frohlich M, Veber M, Girandon L, Davis TR, Weeks AE, Kumamoto CA, Cos P, Coenye T, De Coninck B, Cammue BP, Thevissen K (2014) Plant-derived decapeptide OSIP108 interferes with Candida albicans biofilm formation without affecting cell viability. Antimicrob Agents Chemother 58:2647–2656. https://doi.org/10.1128/aac.01274-13
Ding Y, Wang W, Fan M, Tong Z, Kuang R, Jiang W, Ni L (2014) Antimicrobial and anti-biofilm effect of Bac8c on major bacteria associated with dental caries and Streptococcus mutans biofilms. Peptides 52:61–67. https://doi.org/10.1016/j.peptides.2013.11.020
Dubern JF, Lugtenberg BJ, Bloemberg GV (2006) The ppuI-rsaL-ppuR quorum-sensing system regulates biofilm formation of Pseudomonas putida PCL1445 by controlling biosynthesis of the cyclic lipopeptides putisolvins I and II. J Bacteriol 188:2898–2906. https://doi.org/10.1128/jb.188.8.2898-2906.2006
Eckert R, He J, Yarbrough DK, Qi F, Anderson MH, Shi W (2006) Targeted killing of Streptococcus mutans by a pheromone-guided “smart” antimicrobial peptide. Antimicrob Agents Chemother 50:3651–3657. https://doi.org/10.1128/aac.00622-06
Feng X, Sambanthamoorthy K, Palys T, Paranavitana C (2013) The human antimicrobial peptide LL-37 and its fragments possess both antimicrobial and antibiofilm activities against multidrug-resistant Acinetobacter baumannii. Peptides 49:131–137. https://doi.org/10.1016/j.peptides.2013.09.007
Flemming HC, Wingender J (2010) The biofilm matrix. Nat Rev Microbiol 8:623–633. https://doi.org/10.1038/nrmicro2415
Fong JN, Yildiz FH (2015) Biofilm matrix proteins. Microbiol Spectr 3. https://doi.org/10.1128/microbiolspec.MB-0004-2014
Gopal R, Lee JH, Kim YG, Kim MS, Seo CH, Park Y (2013) Anti-microbial, anti-biofilm activities and cell selectivity of the NRC-16 peptide derived from witch flounder, Glyptocephalus cynoglossus. Mar Drugs 11:1836–1852. https://doi.org/10.3390/md11061836
Gopal R, Kim YG, Lee JH, Lee SK, Chae JD, Son BK, Seo CH, Park Y (2014) Synergistic effects and antibiofilm properties of chimeric peptides against multidrug-resistant Acinetobacter baumannii strains. Antimicrob Agents Chemother 58:1622–1629. https://doi.org/10.1128/aac.02473-13
Gui Z, Wang H, Ding T, Zhu W, Zhuang X, Chu W (2014) Azithromycin reduces the production of alpha-hemolysin and biofilm formation in Staphylococcus aureus. Ind J Microbiol 54:114–117. https://doi.org/10.1007/s12088-013-0438-4
Haisma EM, de Breij A, Chan H, van Dissel JT, Drijfhout JW, Hiemstra PS, El Ghalbzouri A, Nibbering PH (2014) LL-37-derived peptides eradicate multidrug-resistant Staphylococcus aureus from thermally wounded human skin equivalents. Antimicrob Agents Chemother 58:4411–4419. https://doi.org/10.1128/aac.02554-14
Han HM, Gopal R, Park Y (2016) Design and membrane-disruption mechanism of charge-enriched AMPs exhibiting cell selectivity, high-salt resistance, and anti-biofilm properties. Amino Acids 48:505–522. https://doi.org/10.1007/s00726-015-2104-0
He J, Yarbrough DK, Kreth J, Anderson MH, Shi W, Eckert R (2010) Systematic approach to optimizing specifically targeted antimicrobial peptides against Streptococcus mutans. Antimicrob Agents Chemother 54:2143–2151. https://doi.org/10.1128/aac.01391-09
Hirt H, Gorr SU (2013) Antimicrobial peptide GL13K is effective in reducing biofilms of Pseudomonas aeruginosa. Antimicrob Agents Chemother 57:4903–4910. https://doi.org/10.1128/aac.00311-13
Hwang IS, Hwang JS, Hwang JH, Choi H, Lee E, Kim Y, Lee DG (2013) Synergistic effect and antibiofilm activity between the antimicrobial peptide coprisin and conventional antibiotics against opportunistic bacteria. Curr Microbiol 66:56–60. https://doi.org/10.1007/s00284-012-0239-8
Jack AA, Daniels DE, Jepson MA, Vickerman MM, Lamont RJ, Jenkinson HF, Nobbs AH (2015) Streptococcus gordonii comCDE (competence) operon modulates biofilm formation with Candida albicans. Microbiology 161:411–421. https://doi.org/10.1099/mic.0.000010
Kalia VC (2013) Quorum sensing inhibitors: an overview. Biotechnol Adv 31:224–245. https://doi.org/10.1016/j.biotechadv.2012.10.004
Kalia VC (2014) In search of versatile organisms for quorum-sensing inhibitors: acyl homoserine lactones (AHL)-acylase and AHL-lactonase. FEMS Microbiol Lett 359:143. https://doi.org/10.1111/1574-6968.12585
Kanthawong S, Bolscher JG, Veerman EC, van Marle J, Nazmi K, Wongratanacheewin S, Taweechaisupapong S (2010) Antimicrobial activities of LL-37 and its truncated variants against Burkholderia thailandensis. Int J Antimicrob Agents 36:447–452. https://doi.org/10.1016/j.ijantimicag.2010.06.031
Kanthawong S, Bolscher JG, Veerman EC, van Marle J, de Soet HJ, Nazmi K, Wongratanacheewin S, Taweechaisupapong S (2012) Antimicrobial and antibiofilm activity of LL-37 and its truncated variants against Burkholderia pseudomallei. Int J Antimicrob Agents 39:39–44. https://doi.org/10.1016/j.ijantimicag.2011.09.010
Kaplan JB, Ragunath C, Ramasubbu N, Fine DH (2003) Detachment of Actinobacillus actinomycetemcomitans biofilm cells by an endogenous beta-hexosaminidase activity. J Bacteriol 185:4693–4698
Kiran MD, Adikesavan NV, Cirioni O, Giacometti A, Silvestri C, Scalise G, Ghiselli R, Saba V, Orlando F, Shoham M, Balaban N (2008) Discovery of a quorum-sensing inhibitor of drug-resistant staphylococcal infections by structure-based virtual screening. Mol Pharmacol 73:1578–1586. https://doi.org/10.1124/mol.107.044164
Knafl D, Tobudic S, Cheng SC, Bellamy DR, Thalhammer F (2017) Dalbavancin reduces biofilms of methicillin-resistant Staphylococcus aureus (MRSA) and methicillin-resistant Staphylococcus epidermidis (MRSE). Eur J Clin Microbiol Infect Dis 36:677–680. https://doi.org/10.1007/s10096-016-2845-z
Kostakioti M, Hadjifrangiskou M, Hultgren SJ (2013) Bacterial biofilms: development, dispersal, and therapeutic strategies in the dawn of the postantibiotic era. Cold Spring Harb Perspect Med 3:a010306. https://doi.org/10.1101/cshperspect.a010306
Koul S, Kalia VC (2017) Multiplicity of quorum quenching enzymes: A potential mechanism to limit quorum sensing bacterial population. Indian J Microbiol 57:100–108. https://doi.org/10.1007/s12088-016-0633-1
Koul S, Prakash J, Mishra A, Kalia VC (2016) Potential emergence of multi-quorum sensing inhibitor resistant (MQSIR) bacteria. Indian J Microbiol 56:1–18. https://doi.org/10.1007/s12088-015-0558-0
Li YH, Tian X (2012) Quorum sensing and bacterial social interactions in biofilms. Sensors (Basel) 12:2519–2538. https://doi.org/10.3390/s120302519
Li S, Zhu C, Fang S, Zhang W, He N, Xu W, Kong R, Shang X (2015) Ultrasound microbubbles enhance human beta-defensin 3 against biofilms. J Surg Res 199:458–469. https://doi.org/10.1016/j.jss.2015.05.030
Maisetta G, Batoni G, Esin S, Florio W, Bottai D, Favilli F, Campa M (2006) In vitro bactericidal activity of human beta-defensin 3 against multidrug-resistant nosocomial strains. Antimicrob Agents Chemother 50:806–809. https://doi.org/10.1128/aac.50.2.806-809.2006
Martinez LR, Casadevall A (2006) Cryptococcus neoformans cells in biofilms are less susceptible than planktonic cells to antimicrobial molecules produced by the innate immune system. Infect Immun 74:6118–6123. https://doi.org/10.1128/iai.00995-06
Molhoek EM, van Dijk A, Veldhuizen EJ, Haagsman HP, Bikker FJ (2011) A cathelicidin-2-derived peptide effectively impairs Staphylococcus epidermidis biofilms. Int J Antimicrob Agents 37: 476-479. doi:https://doi.org/10.1016/j.ijantimicag.2010.12.020
Montanaro L, Poggi A, Visai L, Ravaioli S, Campoccia D, Speziale P, Arciola CR (2011) Extracellular DNA in biofilms. Int J Artif Organs 34:824–831. https://doi.org/10.5301/ijao.5000051
Morici P, Fais R, Rizzato C, Tavanti A, Lupetti A (2016) Inhibition of Candida albicans biofilm formation by the synthetic lactoferricin derived peptide hLF1-11. PLoS One 11:e0167470. https://doi.org/10.1371/journal.pone.0167470
Nagant C, Pitts B, Nazmi K, Vandenbranden M, Bolscher JG, Stewart PS, Dehaye JP (2012) Identification of peptides derived from the human antimicrobial peptide LL-37 active against biofilms formed by Pseudomonas aeruginosa using a library of truncated fragments. Antimicrob Agents Chemother 56:5698–5708. https://doi.org/10.1128/aac.00918-12
Nijland R, Hall MJ, Burgess JG (2010) Dispersal of biofilms by secreted, matrix degrading, bacterial DNase. PLoS One 5:e15668. https://doi.org/10.1371/journal.pone.0015668
Overhage J, Campisano A, Bains M, Torfs EC, Rehm BH, Hancock RE (2008) Human host defense peptide LL-37 prevents bacterial biofilm formation. Infect Immun 76:4176–4182. https://doi.org/10.1128/iai.00318-08
Parsek MR, Greenberg EP (2005) Sociomicrobiology: the connections between quorum sensing and biofilms. Trends Microbiol 13:27–33. https://doi.org/10.1016/j.tim.2004.11.007
Pletzer D, Hancock RE (2016) Antibiofilm peptides: potential as broad-spectrum agents. J Bacteriol 198:2572–2578. https://doi.org/10.1128/jb.00017-16
Pletzer D, Coleman SR, Hancock RE (2016) Anti-biofilm peptides as a new weapon in antimicrobial warfare. Curr Opin Microbiol 33:35–40. https://doi.org/10.1016/j.mib.2016.05.016
Pusateri CR, Monaco EA, Edgerton M (2009) Sensitivity of Candida albicans biofilm cells grown on denture acrylic to antifungal proteins and chlorhexidine. Arch Oral Biol 54:588–594. https://doi.org/10.1016/j.archoralbio.2009.01.016
Rajput A, Kumar M (2017a) Computational exploration of putative LuxR solos in archaea and their functional implications in quorum sensing. Front Microbiol 8:798. https://doi.org/10.3389/fmicb.2017.00798
Rajput A, Kumar M (2017b) In silico analyses of conservational, functional and phylogenetic distribution of the LuxI and LuxR homologs in Gram-positive bacteria. Sci Rep 7:6969. https://doi.org/10.1038/s41598-017-07241-5
Rajput A, Gupta AK, Kumar M (2015) Prediction and analysis of quorum sensing peptides based on sequence features. PLoS One 10:e0120066. https://doi.org/10.1371/journal.pone.0120066
Rajput A, Kaur K, Kumar M (2016) SigMol: repertoire of quorum sensing signaling molecules in prokaryotes. Nucleic Acids Res 44:D634–D639. https://doi.org/10.1093/nar/gkv1076
Rajput A, Thakur A, Sharma S, Kumar M (2018) aBiofilm: a resource of anti-biofilm agents and their potential implications in targeting antibiotic drug resistance. Nucleic Acids Res 46:D894–d900. https://doi.org/10.1093/nar/gkx1157
Reffuveille F, de la Fuente-Nunez C, Mansour S, Hancock RE (2014) A broad-spectrum antibiofilm peptide enhances antibiotic action against bacterial biofilms. Antimicrob Agents Chemother 58: 5363–5371. doi:https://doi.org/10.1128/aac.03163-14
Sanchez-Gomez S, Ferrer-Espada R, Stewart PS, Pitts B, Lohner K, Martinez de Tejada G (2015) Antimicrobial activity of synthetic cationic peptides and lipopeptides derived from human lactoferricin against Pseudomonas aeruginosa planktonic cultures and biofilms. BMC Microbiol 15:137. https://doi.org/10.1186/s12866-015-0473-x
Sand W, Gehrke T (2006) Extracellular polymeric substances mediate bioleaching/biocorrosion via interfacial processes involving iron(III) ions and acidophilic bacteria. Res Microbiol 157:49–56. https://doi.org/10.1016/j.resmic.2005.07.012
Scarsini M, Tomasinsig L, Arzese A, D’Este F, Oro D, Skerlavaj B (2015) Antifungal activity of cathelicidin peptides against planktonic and biofilm cultures of Candida species isolated from vaginal infections. Peptides 71:211–221. https://doi.org/10.1016/j.peptides.2015.07.023
Singh S, Singh H, Tuknait A, Chaudhary K, Singh B, Kumaran S, Raghava GP (2015) PEPstrMOD: structure prediction of peptides containing natural, non-natural and modified residues. Biol Direct 10:73. https://doi.org/10.1186/s13062-015-0103-4
Stewart PS (2003) Diffusion in biofilms. J Bacteriol 185:1485–1491
Sullivan R, Santarpia P, Lavender S, Gittins E, Liu Z, Anderson MH, He J, Shi W, Eckert R (2011) Clinical efficacy of a specifically targeted antimicrobial peptide mouth rinse: targeted elimination of Streptococcus mutans and prevention of demineralization. Caries Res 45:415–428. https://doi.org/10.1159/000330510
Theberge S, Semlali A, Alamri A, Leung KP, Rouabhia M (2013) C. albicans growth, transition, biofilm formation, and gene expression modulation by antimicrobial decapeptide KSL-W. BMC Microbiol 13:246. https://doi.org/10.1186/1471-2180-13-246
Toyofuku M, Inaba T, Kiyokawa T, Obana N, Yawata Y, Nomura N (2015) Environmental factors that shape biofilm formation. Biosci Biotechnol Biochem 80:7–12. https://doi.org/10.1080/09168451.2015.1058701
Vuotto C, Longo F, Pascolini C, Donelli G, Balice MP, Libori MF, Tiracchia V, Salvia A, Varaldo PE (2017) Biofilm formation and antibiotic resistance in Klebsiella pneumoniae urinary strains. J Appl Microbiol 123:1003–1018. https://doi.org/10.1111/jam.13533
Winfred SB, Meiyazagan G, Panda JJ, Nagendrababu V, Deivanayagam K, Chauhan VS, Venkatraman G (2014) Antimicrobial activity of cationic peptides in endodontic procedures. Eur J Dent 8:254–260. https://doi.org/10.4103/1305-7456.130626
Wingender J, Strathmann M, Rode A, Leis A, Flemming HC (2001) Isolation and biochemical characterization of extracellular polymeric substances from Pseudomonas aeruginosa. Methods Enzymol 336:302–314
Zhou Y, Zhao R, Ma B, Gao H, Xue X, Qu D, Li M, Meng J, Luo X, Hou Z (2016) Oligomerization of RNAIII-inhibiting peptide inhibits adherence and biofilm formation of methicillin-resistant Staphylococcus aureus in vitro and in vivo. Microb Drug Resist 22:193–201. https://doi.org/10.1089/mdr.2015.0170
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2018 Springer Nature Singapore Pte Ltd.
About this chapter
Cite this chapter
Rajput, A., Kumar, M. (2018). Anti-biofilm Peptides: A New Class of Quorum Quenchers and Their Prospective Therapeutic Applications. In: Kalia, V. (eds) Biotechnological Applications of Quorum Sensing Inhibitors. Springer, Singapore. https://doi.org/10.1007/978-981-10-9026-4_5
Download citation
DOI: https://doi.org/10.1007/978-981-10-9026-4_5
Published:
Publisher Name: Springer, Singapore
Print ISBN: 978-981-10-9025-7
Online ISBN: 978-981-10-9026-4
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)