Antimicrobial Peptide against Resistant Bacteria: Comparison
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Please note this is a comparison between Version 2 by Ron Wang and Version 1 by Iván Darío Ocampo-Ibáñez.

The emergence of bacteria resistant to conventional antibiotics is of great concern in modern medicine because it renders ineffectiveness of the current empirical antibiotic therapies. Infections caused by vancomycin-resistant Staphylococcus aureus (VRSA) and vancomycin-intermediate S. aureus (VISA) strains represent a serious threat to global health due to their considerable morbidity and mortality rates. Therefore, there is an urgent need of research and development of new antimicrobial alternatives against these bacteria. In this context, the use of antimicrobial peptides (AMPs) is considered a promising alternative therapeutic strategy to control resistant strains. Therefore, a wide number of natural, artificial, and synthetic AMPs have been evaluated against VRSA and VISA strains, with great potential for clinical application. In this regard, we aimed to present a comprehensive and systematic review of research findings on AMPs that have shown antibacterial activity against vancomycin-resistant and vancomycin-intermediate resistant strains and clinical isolates of S. aureus, discussing their classification and origin, physicochemical and structural characteristics, and possible action mechanisms. This is the first review that includes all peptides that have shown antibacterial activity against VRSA and VISA strains exclusively. 

  • antimicrobial peptides
  • vancomycin-resistant Staphylococcus aureus
  • vancomycin-intermediate resistant Staphylococcus aureus
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References

  1. Fan, Z.; Cao, L.; He, Y.; Hu, J.; Di, Z.; Wu, Y.; Li, W.; Cao, Z. Ctriporin, a new anti-methicillin-resistant Staphylococcus aureus peptide from the venom of the scorpion Chaerilus tricostatus. Antimicrob. Agents Chemother. 2011, 55, 5220–5229.
  2. Miyoshi, N.; Isogai, E.; Hiramatsu, K.; Sasaki, T. Activity of tick antimicrobial peptide from Ixodes persulcatus (persulcatusin) against cell membranes of drug-resistant Staphylococcus aureus. J. Antibiot. (Tokyo) 2017, 70, 142–146.
  3. Jelinkova, P.; Splichal, Z.; Jimenez, A.M.J.; Haddad, Y.; Mazumdar, A.; Sur, V.P.; Milosavljevic, V.; Kopel, P.; Buchtelova, H.; Guran, R.; et al. Novel vancomycin–peptide conjugate as potent antibacterial agent against vancomycin-resistant Staphylococcus aureus. Infect Drug Resist. 2018, 11, 1807–1817.
  4. Saravolatz, L.D.; Pawlak, J.; Johnson, L.; Bonilla, H.; Saravolatz, L.D.; Fakih, M.G.; Fugelli, A.; Olsen, W.M. In Vitro activities of LTX-109, a synthetic antimicrobial peptide, against methicillin-resistant, vancomycin-intermediate, vancomycin-resistant, daptomycin-nonsusceptible, and linezolid-nonsusceptible Staphylococcus aureus. Antimicrob. Agents Chemother. 2012, 56, 4478–4482.
  5. Mohamed, M.F.; Abdelkhalek, A.; Seleem, M.N. Evaluation of short synthetic antimicrobial peptides for treatment of drug-resistant and intracellular Staphylococcus aureus. Sci. Rep. 2016, 6, 1–14.
  6. Regmi, S.; Choi, Y.H.; Choi, Y.S.; Kim, M.R.; Yoo, J.C. Antimicrobial peptide isolated from Bacillus amyloliquefaciens K14 revitalizes its use in combinatorial drug therapy. Folia Microbiol. (Praha) 2017, 62, 127–138.
  7. Regmi, S.; Choi, Y.S.; Choi, Y.H.; Kim, Y.K.; Cho, S.S.; Yoo, J.C.; Suh, J.W. Antimicrobial peptide from Bacillus subtilis CSB138: Characterization, killing kinetics, and synergistic potency. Int. Microbiol. 2017, 20, 45–53.
  8. Azmi, F.; Elliott, A.G.; Marasini, N.; Ramu, S.; Ziora, Z.; Kavanagh, A.M.; Blaskovich, M.A.T.; Cooper, M.A.; Skwarczynski, M.; Toth, I. Short cationic lipopeptides as effective antibacterial agents: Design, physicochemical properties and biological evaluation. Bioorganic Med. Chem. 2016, 24, 2235–2241.
  9. Shurko, J.F.; Galega, R.S.; Li, C.; Lee, G.C. Evaluation of LL-37 antimicrobial peptide derivatives alone and in combination with vancomycin against S. aureus. J. Antibiot. 2018, 71, 971–974.
  10. Fritsche, T.R.; Rhomberg, P.R.; Sader, H.S.; Jones, R.N. In Vitro activity of omiganan pentahydrochloride tested against vancomycin-tolerant, -intermediate, and -resistant Staphylococcus aureus. Diagn. Microbiol. Infect Dis. 2008, 60, 399–403.
  11. Wu, C.; Hsueh, J.; Yip, B.; Chih, Y.; Peng, K.; Cheng, J. Antimicrobial Peptides Display Strong Synergy with Vancomycin Against Vancomycin-Resistant. Int. J. Mol. Sci. 2020, 21, 4578.
  12. Ghobrial, O.G.; Derendorf, H.; Hillman, J.D. Pharmacodynamic activity of the lantibiotic MU1140. Int. J. Antimicrob. Agents 2009, 33, 70–74.
  13. Choi, Y.H.; Cho, S.S.; Simkhada, J.R.; Yoo, J.C. A novel thermotolerant and acidotolerant peptide produced by a Bacillus strain newly isolated from a fermented food (kimchi) shows activity against multidrug-resistant bacteria. Int. J. Antimicrob. Agents 2012, 40, 80–83.
  14. Bédard, F.; Fliss, I.; Biron, E. Structure-Activity Relationships of the Bacteriocin Bactofencin A and Its Interaction with the Bacterial Membrane. ACS Infect Dis. 2019, 5, 199–207.
  15. Wang, B.; Yao, Y.; Wei, P.; Song, C.; Wan, S.; Yang, S.; Zhu, G.M.; Liu, H.M. Housefly Phormicin inhibits Staphylococcus aureus and MRSA by disrupting biofilm formation and altering gene expression In Vitro and In Vivo. Int. J. Biol. Macromol. 2020.
  16. Mohamed, M.F.; Hamed, M.I.; Panitch, A.; Seleem, M.N. Targeting methicillin-resistant Staphylococcus aureus with short salt-resistant synthetic peptides. Antimicrob. Agents Chemother. 2014, 58, 4113–4122.
  17. Muller, J.A.I.; Lawrence, N.; Chan, L.Y.; Harvey, P.J.; Elliott, A.G.; Blaskovich, M.A.T.; Gonçalves, J.C.; Galante, P.; Mortari, M.R.; Toffoli-Kadri, M.C.; et al. Antimicrobial and Anticancer Properties of Synthetic Peptides Derived from the Wasp Parachartergus fraternus. Chem. Biol. Chem. 2021, 22, 1415–1423.
  18. Cirioni, O.; Silvestri, C.; Ghiselli, R.; Giacometti, A.; Orlando, F.; Mocchegiani, F.; Chiodi, L.; Della Vittoria, A.; Saba, V.; Scalise, G. Experimental study on the efficacy of combination of α-helical antimicrobial peptides and vancomycin against Staphylococcus aureus with intermediate resistance to glycopeptides. Peptides 2006, 27, 2600–2606.
  19. Lima, W.G.; de Brito, J.C.M.; Cardoso, V.N.; Fernandes, S.O.A. In-depth characterization of antibacterial activity of melittin against Staphylococcus aureus and use in a model of non-surgical MRSA-infected skin wounds. Eur. J. Pharm. Sci. 2021, 156, 105592.
  20. Wenzel, M.; Prochnow, P.; Mowbray, C.; Vuong, C.; Höxtermann, S.; Stepanek, J.J.; Albada, H.B.; Hall, J.; Metzler-Nolte, N.; Bandow, J.E. Towards profiles of resistance development and toxicity for the small cationic hexapeptide RWRWRW-NH 2. Front. Cell Dev. Biol. 2016, 4, 1–9.
  21. Kim, P.I.; Sohng, J.K.; Sung, C.; Joo, H.S.; Kim, E.M.; Yamaguchi, T.; Park, D.; Kim, B.G. Characterization and structure identification of an antimicrobial peptide, hominicin, produced by Staphylococcus hominis MBBL 2-9. Biochem. Biophys. Res. Commun. 2010, 399, 133–138.
  22. Piper, C.; Draper, L.A.; Cotter, P.D.; Ross, R.P.; Hill, C. A comparison of the activities of lacticin 3147 and nisin against drug-resistant Staphylococcus aureus and Enterococcus species. J. Antimicrob. Chemother. 2009, 64, 546–551.
  23. Harrison, P.L.; Abdel-Rahman, M.A.; Strong, P.N.; Tawfik, M.M.; Miller, K. Characterisation of three alpha-helical antimicrobial peptides from the venom of Scorpio maurus palmatus. Toxicon 2016, 117, 30–36.
  24. Sass, P.; Jansen, A.; Szekat, C.; Sass, V.; Sahl, H.G.; Bierbaum, G. The lantibiotic mersacidin is a strong inducer of the cell wall stress response of Staphylococcus aureus. BMC Microbiol. 2008, 8, 1–11.
  25. Mishra, B.; Wang, X.; Lushnikova, T.; Zang, Y.; Golla, R.; Lakshmaiah, J.; Wang, C.; Mcguire, T.; Wang, G. Antibacterial, Antifungal, Anticancer Activities and Structural Bioinformatics Analysis of Six Naturally Occurring Temporins. Peptides 2018, 1, 9–20.
  26. Bionda, N.; Stawikowski, M.; Stawikowski, R.; Cudic, M.; Lopéz, F.; Treitl, D.; Medina, J.; Cudic, P. Effects of cyclic lipodepsipeptide structural modulation on stability, antibacterial activity and human cell toxicity. Chem. Med. Chem. 2012, 7, 871–882.
  27. Zipperer, A.; Konnerth, M.C.; Laux, C.; Berscheid, A.; Janek, D.; Weidenmaier, C.; Burian, M.; Schilling, N.A.; Slavetinsky, C.; Marschal, M.; et al. Human commensals producing a novel antibiotic impair pathogen colonization. Nature 2016, 535, 511–516.
  28. Mishra, B.; Lushnikova, T.; Wang, G. Small lipopeptides possess anti-biofilm capability comparable to daptomycin and vancomycin. RSC Adv. 2015, 5, 59758–59769.
  29. Nielsen, S.L.; Frimodt-Møller, N.; Kragelund, B.B.; Hansen, P.R. Structure-activity study of the antibacterial peptide fallaxin. Protein Sci. 2007, 16, 1969–1976.
  30. Mojsoska, B.; Jenssen, H. Peptides and peptidomimetics for antimicrobial drug design. Pharmaceuticals 2015, 8, 366–415.
  31. National Center for Biotechnology Information. PubChem Compound Summary for CID 16131446, Omiganan Pentahydrochloride. Available online: (accessed on 3 June 2021).
  32. Makarova, O.; Johnston, P.; Rodriguez-Rojas, A.; El Shazely, B.; Morales, J.M.; Rolff, J. Genomics of experimental adaptation of Staphylococcus aureus to a natural combination of insect antimicrobial peptides. Sci. Rep. 2018, 8, 15359.
  33. El Shazely, B.; Yu, G.; Johnston, P.R.; Rolff, J. Resistance Evolution Against Antimicrobial Peptides in Staphylococcus aureus Alters Pharmacodynamics Beyond the MIC. Front. Microbiol. 2020, 11, 103.
  34. Garoy, E.Y.; Gebreab, Y.B.; Achila, O.O.; Tekeste, D.G.; Kesete, R.; Ghirmay, R.; Kiflay, R.; Tesfu, T. Methicillin-Resistant Staphylococcus aureus (MRSA): Prevalence and Antimicrobial Sensitivity Pattern among Patients—A Multicenter Study in Asmara, Eritrea. Can. J. Infect Dis. Med. Microbiol. 2019, 2019.
  35. Steinig, E.J.; Duchene, S.; Robinson, D.A.; Monecke, S.; Yokoyama, M.; Laabei, M.; Slickers, P.; Andersson, P.; Williamson, D.; Kearns, A.; et al. Evolution and global transmission of a multidrug-resistant, community-associated methicillin-resistant staphylococcus aureus lineage from the Indian subcontinent. MBio 2019, 10, 1–20.
  36. Parastan, R.; Kargar, M.; Solhjoo, K.; Kafilzadeh, F. A synergistic association between adhesion-related genes and multidrug resistance patterns of Staphylococcus aureus isolates from different patients and healthy individuals. J. Glob. Antimicrob. Resist. 2020, 22, 379–385.
  37. Farrell, D.J.; Flamm, R.K.; Sader, H.S.; Jones, R.N. Activity of ceftobiprole against methicillin-resistant Staphylococcus aureus strains with reduced susceptibility to daptomycin, linezolid or vancomycin, and strains with defined SCCmec types. Int. J. Antimicrob. Agents 2014, 43, 323–327.
  38. Shekarabi, M.; Hajikhani, B.; Salimi Chirani, A.; Fazeli, M.; Goudarzi, M. Molecular characterization of vancomycin-resistant Staphylococcus aureus strains isolated from clinical samples: A three year study in Tehran, Iran. PLoS ONE 2017, 12, e0183607.
  39. Reichmann, N.T.; Pinho, M.G. Role of SCCmec type in resistance to the synergistic activity of oxacillin and cefoxitin in MRSA. Sci. Rep. 2017, 7, 1–9.
  40. Katayama, Y.; Ito, T.; Hiramatsu, K. A new class of genetic element, staphylococcus cassette chromosome mec, encodes methicillin resistance in Staphylococcus aureus. Antimicrob. Agents Chemother. 2000, 44, 1549–1555.
  41. BARBER, M. Methicillin-resistant staphylococci. J. Clin. Pathol. 1961, 14, 385–393.
  42. Hiramatsu, K.; Katayama, Y.; Matsuo, M.; Sasaki, T.; Morimoto, Y.; Sekiguchi, A.; Baba, T. Multi-drug-resistant Staphylococcus aureus and future chemotherapy. J. Infect Chemother 2014, 20, 593–601.
  43. Chambers, H.F. Methicillin resistance in staphylococci: Molecular and biochemical basis and clinical implications. Clin. Microbiol. Rev. 1997, 10, 781–791.
  44. Ito, T.; Katayama, Y.; Asada, K.; Mori, N.; Tsutsumimoto, K.; Tiensasitorn, C.; Hiramatsu, K. Structural comparison of three types of staphylococcal cassette chromosome mec integrated in the chromosome in methicillin-resistant Staphylococcus aureus. Antimicrob. Agents Chemother. 2001, 45, 1323–1336.
  45. Miragaia, M. Factors contributing to the evolution of Meca-mediated β-lactam resistance in staphylococci: Update and new insights from whole genome sequencing (WGS). Front. Microbiol. 2018, 9, 2723.
  46. Mella, S.S. Staphylococcus aureus resistente a vancomicina. Rev. Chil. Infectol. 2002, 19, 575–587.
  47. CLSI. Performance Standards for Antimicrobial Susceptibility Testing; Twenty-Seventh Informational Supplement, CLSI Document M100-S27; Clinical and Laboratory Standards Institute: Wayne, PA, USA, 2017; ISBN 1562387855.
  48. Cong, Y.; Yang, S.; Rao, X. Vancomycin resistant Staphylococcus aureus infections: A review of case updating and clinical features. J. Adv. Res. 2020, 21, 169–176.
  49. McGuinness, W.A.; Malachowa, N.; DeLeo, F.R. Vancomycin resistance in Staphylococcus aureus. Yale J. Biol. Med. 2017, 90, 269–281.
  50. Loomba, P.; Taneja, J.; Mishra, B. Methicillin and vancomycin resistant S. aureus in hospitalized patients. J. Glob. Infect Dis. 2010, 2, 275.
  51. Wenzel, M.; Prochnow, P.; Mowbray, C.; Vuong, C.; Höxtermann, S.; Stepanek, J.J.; Albada, H.B.; Hall, J.; Metzler-Nolte, N.; Bandow, J.E. Towards profiles of resistance development and toxicity for the small cationic hexapeptide RWRWRW-NH 2. Front. Cell Dev. Biol. 2016, 4, 1–9.
  52. Howden, B.P.; Davies, J.K.; Johnson, P.D.R.; Stinear, T.P.; Grayson, M.L. Reduced vancomycin susceptibility in Staphylococcus aureus, including vancomycin-intermediate and heterogeneous vancomycin-intermediate strains: Resistance mechanisms, laboratory detection, and clinical implications. Clin. Microbiol. Rev. 2010, 23, 99–139.
  53. Chaili, S.; Cheung, A.L.; Bayer, A.S.; Xiong, Y.Q.; Waring, A.J.; Memmi, G.; Donegan, N.; Yang, S.J.; Yeaman, M.R. The GraS sensor in Staphylococcus aureus mediates resistance to host defense peptides differing in mechanisms of action. Infect Immun. 2016, 84, 459–466.
  54. Wang, J.; Dou, X.; Song, J.; Lyu, Y.; Zhu, X.; Xu, L.; Li, W.; Shan, A. Antimicrobial peptides: Promising alternatives in the post feeding antibiotic era. Med. Res. Rev. 2018, 39, 831–859.
  55. Zelezetsky, I.; Tossi, A. Alpha-helical antimicrobial peptides-Using a sequence template to guide structure-activity relationship studies. Biochim. Biophys. Acta Biomembr. 2006, 1758, 1436–1449.
  56. Mojsoska, B.; Jenssen, H. Peptides and peptidomimetics for antimicrobial drug design. Pharmaceuticals 2015, 8, 366–415.
  57. Wu, Q.; Patočka, J.; Kuča, K. Insect Antimicrobial Peptides, a Mini Review. Toxins 2018, 10, 461.
  58. Sancho-Vaello, E.; Gil-Carton, D.; François, P.; Bonetti, E.J.; Kreir, M.; Pothula, K.R.; Kleinekathöfer, U.; Zeth, K. The structure of the antimicrobial human cathelicidin LL-37 shows oligomerization and channel formation in the presence of membrane mimics. Sci. Rep. 2020, 10, 1–16.
  59. Muller, J.A.I.; Lawrence, N.; Chan, L.Y.; Harvey, P.J.; Elliott, A.G.; Blaskovich, M.A.T.; Gonçalves, J.C.; Galante, P.; Mortari, M.R.; Toffoli-Kadri, M.C.; et al. Antimicrobial and Anticancer Properties of Synthetic Peptides Derived from the Wasp Parachartergus fraternus. Chem. Biol. Chem. 2021, 22, 1415–1423.
  60. Seil, M.; Nagant, C.; Dehaye, J.P.; Vandenbranden, M.; Lensink, M.F. Spotlight on human LL-37, an immunomodulatory peptide with promising cell-penetrating properties. Pharmaceuticals 2010, 3, 3435–3460.
  61. Raghuraman, H.; Chattopadhyay, A. Melittin: A membrane-active peptide with diverse functions. Biosci. Rep. 2007, 27, 189–223.
  62. Ceremuga, M.; Stela, M.; Janik, E.; Gorniak, L.; Synowiec, E.; Sliwinski, T.; Sitarek, P.; Saluk-Bijak, J.; Bijak, M. Melittin—a natural peptide from bee venom which induces apoptosis in human leukaemia cells. Biomolecules 2020, 10, 247.
  63. Jelinkova, P.; Splichal, Z.; Jimenez, A.M.J.; Haddad, Y.; Mazumdar, A.; Sur, V.P.; Milosavljevic, V.; Kopel, P.; Buchtelova, H.; Guran, R.; et al. Novel vancomycin–peptide conjugate as potent antibacterial agent against vancomycin-resistant Staphylococcus aureus. Infect Drug Resist. 2018, 11, 1807–1817.
  64. Harrison, P.L.; Abdel-Rahman, M.A.; Strong, P.N.; Tawfik, M.M.; Miller, K. Characterisation of three alpha-helical antimicrobial peptides from the venom of Scorpio maurus palmatus. Toxicon 2016, 117, 30–36.
  65. Matsuzaki, K.; Sugishita, K.I.; Harada, M.; Fujii, N.; Miyajima, K. Interactions of an antimicrobial peptide, magainin 2, with outer and inner membranes of Gram-negative bacteria. Biochim. Biophys. Acta Biomembr. 1997, 1327, 119–130.
  66. Mishra, B.; Wang, X.; Lushnikova, T.; Zang, Y.; Golla, R.; Lakshmaiah, J.; Wang, C.; Mcguire, T.; Wang, G. Antibacterial, Antifungal, Anticancer Activities and Structural Bioinformatics Analysis of Six Naturally Occurring Temporins. Peptides 2018, 1, 9–20.
  67. Nielsen, S.L.; Frimodt-Møller, N.; Kragelund, B.B.; Hansen, P.R. Structure-activity study of the antibacterial peptide fallaxin. Protein Sci. 2007, 16, 1969–1976.
  68. Regmi, S.; Choi, Y.H.; Choi, Y.S.; Kim, M.R.; Yoo, J.C. Antimicrobial peptide isolated from Bacillus amyloliquefaciens K14 revitalizes its use in combinatorial drug therapy. Folia Microbiol. (Praha) 2017, 62, 127–138.
  69. Ennahar, S.; Sashihara, T.; Sonomoto, K.; Ishizaki, A. Class IIa bacteriocins: Biosynthesis, structure and activity. FEMS Microbiol. Rev. 2000, 24, 85–106.
  70. Müller, A.; Wenzel, M.; Strahl, H.; Grein, F.; Saaki, T.N.V.; Kohl, B.; Siersma, T.; Bandow, J.E.; Sahl, H.G.; Schneider, T.; et al. Daptomycin inhibits cell envelope synthesis by interfering with fluid membrane microdomains. Proc. Natl. Acad. Sci. USA 2016, 113, E7077–E7086.
  71. Mohamed, M.F.; Abdelkhalek, A.; Seleem, M.N. Evaluation of short synthetic antimicrobial peptides for treatment of drug-resistant and intracellular Staphylococcus aureus. Sci. Rep. 2016, 6, 1–14.
  72. Mohamed, M.F.; Hamed, M.I.; Panitch, A.; Seleem, M.N. Targeting methicillin-resistant Staphylococcus aureus with short salt-resistant synthetic peptides. Antimicrob. Agents Chemother. 2014, 58, 4113–4122.
  73. Kumar, P.; Kizhakkedathu, J.N.; Straus, S.K. Antimicrobial peptides: Diversity, mechanism of action and strategies to improve the activity and biocompatibility In Vivo. Biomolecules 2018, 8, 4.
  74. Zhong, G.; Cheng, J.; Liang, Z.C.; Xu, L.; Lou, W.; Bao, C.; Ong, Z.Y.; Dong, H.; Yang, Y.Y.; Fan, W. Short Synthetic β-Sheet Antimicrobial Peptides for the Treatment of Multidrug-Resistant Pseudomonas aeruginosa Burn Wound Infections. Adv. Healthc. Mater. 2017, 6.
  75. Jin, Y.; Hammer, J.; Pate, M.; Zhang, Y.; Zhu, F.; Zmuda, E.; Blazyk, J. Antimicrobial activities and structures of two linear cationic peptide families with various amphipathic β-sheet and α-helical potentials. Antimicrob. Agents Chemother. 2005, 49, 4957–4964.
  76. Rausch, J.M.; Marks, J.R.; Wimley, W.C. Rational combinatorial design of pore-forming β-sheet peptides. Proc. Natl. Acad. Sci. USA 2005, 102, 10511–10515.
  77. Santos-Silva, C.A.; Zupin, L.; Oliveira-Lima, M.; Vilela, L.M.; Bezerra-Neto, J.P.; Ferreira-Neto, J.R.; Ferreira, J.D.; Oliveira-Silva, R.L.; Pires, C.D.; Aburjaile, F.F.; et al. Plant Antimicrobial Peptides: State of the Art, In Silico Prediction and Perspectives in the Omics Era. Bioinform. Biol. Insights 2020, 14.
  78. Greco, S.; Gerdol, M.; Edomi, P.; Pallavicini, A. Molecular Diversity of Mytilin-Like Defense Peptides (Mollusca, Bivalvia). Antibiotics 2020, 9, 37.
  79. Dias, R.D.O.; Franco, O.L. Cysteine-stabilized αβ defensins: From a common fold to antibacterial activity. Peptides 2015, 72, 64–72.
  80. Wang, B.; Yao, Y.; Wei, P.; Song, C.; Wan, S.; Yang, S.; Zhu, G.M.; Liu, H.M. Housefly Phormicin inhibits Staphylococcus aureus and MRSA by disrupting biofilm formation and altering gene expression In Vitro and In Vivo. Int. J. Biol. Macromol. 2020.
  81. Simons, A.; Alhanout, K.; Duval, R.E. Bacteriocins, antimicrobial peptides from bacterial origin: Overview of their biology and their impact against multidrug-resistant bacteria. Microorganisms 2020, 8, 639.
  82. Lee, D.W.; Kim, B.S. Antimicrobial cyclic peptides for plant disease control. Plant. Pathol. J. 2015, 31, 1–11.
  83. Jeong Hee, J.; Ha Chul, S. Crystal Structure of NisI in a Lipid-Free Form, the Nisin Immunity Protein, from Lactococcus lactis. Antimicrob. Agents Chemother. 2018, 62, 1–12.
  84. Williams, G.C.; Delves-Broughton, J. NISIN. In Encyclopedia of Food Sciences and Nutrition, 2nd ed.; Caballero, B., Ed.; Academic Press: Oxford, UK, 2003; pp. 4128–4135. ISBN 978-0-12-227055-0.
  85. Sass, P.; Jansen, A.; Szekat, C.; Sass, V.; Sahl, H.G.; Bierbaum, G. The lantibiotic mersacidin is a strong inducer of the cell wall stress response of Staphylococcus aureus. BMC Microbiol. 2008, 8, 1–11.
  86. Smith, L.; Zachariah, C.; Thirumoorthy, R.; Rocca, J.; Novák, J.; Hillman, J.D.; Edison, A.S. Structure and dynamics of the lantibiotic mutacin 1140. Biochemistry 2003, 42, 10372–10384.
  87. Kim, P.I.; Sohng, J.K.; Sung, C.; Joo, H.S.; Kim, E.M.; Yamaguchi, T.; Park, D.; Kim, B.G. Characterization and structure identification of an antimicrobial peptide, hominicin, produced by Staphylococcus hominis MBBL 2-9. Biochem. Biophys. Res. Commun. 2010, 399, 133–138.
  88. O’Shea, E.F.; O’Connor, P.M.; O’Sullivan, O.; Cotter, P.D.; Ross, R.P.; Hill, C. Bactofencin A, a new type of cationic bacteriocin with Unusual Immunity. MBio 2013, 4, 1–9.
  89. Choi, Y.H.; Cho, S.S.; Simkhada, J.R.; Yoo, J.C. A novel thermotolerant and acidotolerant peptide produced by a Bacillus strain newly isolated from a fermented food (kimchi) shows activity against multidrug-resistant bacteria. Int. J. Antimicrob. Agents 2012, 40, 80–83.
  90. Zipperer, A.; Konnerth, M.C.; Laux, C.; Berscheid, A.; Janek, D.; Weidenmaier, C.; Burian, M.; Schilling, N.A.; Slavetinsky, C.; Marschal, M.; et al. Human commensals producing a novel antibiotic impair pathogen colonization. Nature 2016, 535, 511–516.
  91. Bionda, N.; Stawikowski, M.; Stawikowski, R.; Cudic, M.; Lopéz, F.; Treitl, D.; Medina, J.; Cudic, P. Effects of cyclic lipodepsipeptide structural modulation on stability, antibacterial activity and human cell toxicity. Chem. Med. Chem. 2012, 7, 871–882.
  92. Lei, J.; Sun, L.C.; Huang, S.; Zhu, C.; Li, P.; He, J.; Mackey, V.; Coy, D.H.; He, Q.Y. The antimicrobial peptides and their potential clinical applications. Am. J. Transl. Res. 2019, 11, 3919–3931.
  93. Fritsche, T.R.; Rhomberg, P.R.; Sader, H.S.; Jones, R.N. In Vitro activity of omiganan pentahydrochloride tested against vancomycin-tolerant, -intermediate, and -resistant Staphylococcus aureus. Diagn. Microbiol. Infect Dis. 2008, 60, 399–403.
  94. Rubinchik, E.; Dugourd, D. Omiganan Pentahydrochloride: A Novel, Broad-Spectrum Antimicrobial Peptide for Topical Use; Wiley-VCH Verlag GmbH & Co, Boschstr.: Weinheim, Germany, 2011; pp. 157–169. ISBN 9783527328918.
  95. Yu, H.-Y.; Tu, C.-H.; Yip, B.-S.; Chen, H.-L.; Cheng, H.-T.; Huang, K.-C.; Lo, H.-J.; Cheng, J.-W. Easy strategy to increase salt resistance of antimicrobial peptides. Antimicrob. Agents Chemother. 2011, 55, 4918–4921.
  96. Wu, C.; Hsueh, J.; Yip, B.; Chih, Y.; Peng, K.; Cheng, J. Antimicrobial Peptides Display Strong Synergy with Vancomycin Against Vancomycin-Resistant. Int. J. Mol. Sci. 2020, 21, 4578.
  97. Azmi, F.; Elliott, A.G.; Marasini, N.; Ramu, S.; Ziora, Z.; Kavanagh, A.M.; Blaskovich, M.A.T.; Cooper, M.A.; Skwarczynski, M.; Toth, I. Short cationic lipopeptides as effective antibacterial agents: Design, physicochemical properties and biological evaluation. Bioorganic Med. Chem. 2016, 24, 2235–2241.
  98. Datta, S.; Roy, A. Antimicrobial Peptides as Potential Therapeutic Agents: A Review. Int. J. Pept. Res. Ther. 2021, 27, 555–577.
  99. Martinez de Tejada, G.; Sanchez-Gomez, S.; Razquin-Olazaran, I.; Kowalski, I.; Kaconis, Y.; Heinbockel, L.; Andra, J.; Schurholz, T.; Hornef, M.; Dupont, A.; et al. Bacterial Cell Wall Compounds as Promising Targets of Antimicrobial Agents I. Antimicrobial Peptides and Lipopolyamines. Curr. Drug Targets 2012, 13, 1121–1130.
  100. Malanovic, N.; Lohner, K. Antimicrobial Peptides Targeting Gram-Positive Bacteria. Pharmaceuticals 2016, 9, 59.
  101. Ren, H.; Gray, W.M. Amino Acid Composition Determines Peptide Activity Spectrum and Hot-Spot-Based Design of Merecidin. Physiol. Behav. 2019, 176, 139–148.
  102. Yin, L.M.; Edwards, M.A.; Li, J.; Yip, C.M.; Deber, C.M. Roles of hydrophobicity and charge distribution of cationic antimicrobial peptides in peptide-membrane interactions. J. Biol. Chem. 2012, 287, 7738–7745.
  103. Sohlenkamp, C.; Geiger, O. Bacterial membrane lipids: Diversity in structures and pathways. FEMS Microbiol. Rev. 2015, 40, 133–159.
  104. Van Den Bogaart, G.; Guzmán, J.V.; Mika, J.T.; Poolman, B. On the mechanism of pore formation by melittin. J. Biol. Chem. 2008, 283, 33854–33857.
  105. Matsuzaki, K.; Sugishita, K.; Ishibe, N.; Ueha, M.; Nakata, S.; Miyajima, K.; Epand, R.M. Relationship of Membrane Curvature to the Formation of Pores by Magainin 2. Biochemistry 1998, 37, 11856–11863.
  106. Miyoshi, N.; Isogai, E.; Hiramatsu, K.; Sasaki, T. Activity of tick antimicrobial peptide from Ixodes persulcatus (persulcatusin) against cell membranes of drug-resistant Staphylococcus aureus. J. Antibiot. (Tokyo) 2017, 70, 142–146.
  107. Ghobrial, O.G.; Derendorf, H.; Hillman, J.D. Pharmacodynamic activity of the lantibiotic MU1140. Int. J. Antimicrob. Agents 2009, 33, 70–74.
  108. Subbalakshmi, C.; Sitaram, N. Mechanism of antimicrobial action of indolicidin. FEMS Microbiol. Lett. 1998, 160, 91–96.
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