ANTIMICROBIAL PEPTIDES AND TEMPORIN FAMILY IN THE CONTEXT OF RISING RESISTANCE - VIEW ON CURRENT DEVELOPMENT
DOI:
https://doi.org/10.59957/jctm.v61.i3.2026.1Keywords:
antimicrobial resistance, antimicrobial peptides, temporin, temporin A, unnatural amino acids.Abstract
Antimicrobial resistance has surfaced as a gradual yet progressively significant threat to global public health, frequently overshadowed by more widely pressing issues like cancer and cardiovascular disease. Nonetheless, the rapid proliferation of multidrug-resistant pathogens has gathered worldwide attention, prompting organizations like the World Health Organization to classify it as one of the most urgent challenges that modern medicine must face. The reduced efficacy of conventional antibiotics has led to increasing treatment failures, prolonged hospitalizations, and elevated mortality rates, highlighting the urgent need for novel therapeutic approaches. In response to this, there is an increasing interest in overcoming the limitations of conventional antibiotics by developing novel treatment alternatives. Among these alternatives, antimicrobial peptides have attracted considerable attention due to their broad-spectrum efficacy, which includes antibacterial, antiviral, antitumour activities, alongside a unique mechanism of action, coupled with reduced likelihood of inducing resistance. The Temporin family is one of the groups in this category. It was originally isolated from amphibian skin secretions and has shown significant potential as a new source of antibacterial, antiviral, and antifungal agents. Temporins show strong antibacterial properties, particularly against Gram-positive bacteria. Their simple structures make them attractive candidates for enhancement and therapeutic applications. Ongoing research on temporins and other AMPs holds great promise for finding a solution to the global problem of antimicrobial resistance and for shaping the next generation of infection-fighting therapeutics.
References
G.A. Durand, D. Raoult, G. Dubourg, Antibiotic discovery: history, methods and perspectives, Int. J. Antimicrob. Agents, 53, 2019, 371-382.
Md.A. Salam, Md.Y. Al-Amin, M.T. Salam, J.S. Pawar, N. Akhter, A.A. Rabaan, M.A.A. Alqumber, Antimicrobial Resistance: A Growing Serious Threat for Global Public Health, Healthcare, 11, 2023, 1946.
C.J.L. Murray, K.S. Ikuta, F. Sharara, L. Swetschinski, G. Robles Aguilar, A. Gray, C. Han, C. Bisignano, P. Rao, E. Wool, et al, Global burden of bacterial antimicrobial resistance in 2019: a systematic analysis, The Lancet, 399, 2022, 629-655.
J. Davies, D. Davies, Origins and Evolution of Antibiotic Resistance, Microbiol. Mol. Biol. Rev., 74, 2010, 417-433.
E. Christaki, M. Marcou, A. Tofarides, Antimicrobial Resistance in Bacteria: Mechanisms, Evolution, and Persistence, J. Mol. Evol. 88, 2020, 26-40.
N. Bano, S. Parveen, M. Saeed, S. Siddiqui, M. Abohassan, S.S. Mir, Drug Repurposing of Selected Antibiotics: An Emerging Approach in Cancer Drug Discovery, ACS Omega, 9, 2024, 26762-26779.
A. Beberok, D. Wrześniok, J. Rok, Z. Rzepka, M. Respondek, E. Buszman, Ciprofloxacin triggers the apoptosis of human triple-negative breast cancer MDA-MB-231 cells via the p53/Bax/Bcl-2 signaling pathway, Int. J. Oncol., 2018.
Y. Gao, Q. Shang, W. Li, W. Guo, A. Stojadinovic, C. Mannion, Y. Man, T. Chen, Antibiotics for cancer treatment: A double-edged sword, J. Cancer, 11, 2020, 5135-5149.
M.E. Oliver, T.S.C. Hinks, Azithromycin in viral infections, Rev. Med. Virol., 31, 2021, e2163.
B. Deslouches, Y.P. Di, Antimicrobial peptides with selective antitumor mechanisms: prospect for anticancer applications, Oncotarget, 8, 2017, 46635-46651.
M.M. Javadpour, M.M. Juban, W.-C.J. Lo, S.M. Bishop, J.B. Alberty, S.M. Cowell, C.L. Becker, M.L. McLaughlin, De Novo Antimicrobial Peptides with Low Mammalian Cell Toxicity, J. Med. Chem., 39, 1996, 3107-3113.
J.C. Mai, Z. Mi, S.H. Kim, B. Ng, P.D. Robbins, A proapoptotic peptide for the treatment of solid tumors, Cancer Res., 61, 2001, 7709-7712.
C. Oelkrug, M. Hartke, A. Schubert, Mode of action of anticancer peptides (ACPs) from amphibian origin, Anticancer Res., 35, 2015, 635-643.
C. Zhang, M. Yang, Antimicrobial Peptides: From Design to Clinical Application, Antibiotics, 11, 2022, 349.
E.Y. Klein, T.P. Van Boeckel, E.M. Martinez, S. Pant, S. Gandra, S.A. Levin, H. Goossens, R. Laxminarayan, Global increase and geographic convergence in antibiotic consumption between 2000 and 2015, Proc. Natl. Acad. Sci., 115, 2018.
J.A. Ayukekbong, M. Ntemgwa, A.N. Atabe, The threat of antimicrobial resistance in developing countries: causes and control strategies, Antimicrob. Resist. Infect. Control, 6, 2017, 47.
M.E. Velazquez-Meza, M. Galarde-López, B. Carrillo-Quiróz, C.M. Alpuche-Aranda, Antimicrobial resistance: One Health approach, Vet. World, 2022, 743-749.
G. Zhou, Q.-S. Shi, X.-M. Huang, X.-B. Xie, The Three Bacterial Lines of Defense against Antimicrobial Agents, Int. J. Mol. Sci., 16, 2015, 21711-21733.
M. Frieri, K. Kumar, A. Boutin, Antibiotic resistance, J. Infect. Public Health, 10, 2017, 369-378.
J.S. Bradley, J. Garau, H. Lode, K.V.I. Rolston, S.E. Wilson, J.P. Quinn, Carbapenems in clinical practice: a guide to their use in serious infection, Int. J. Antimicrob. Agents, 11, 1999, 93-100.
J. Lei, L. Sun, S. Huang, C. Zhu, P. Li, J. He, V. Mackey, D.H. Coy, Q. He, The antimicrobial peptides and their potential clinical applications, Am. J. Transl. Res., 11, 2019, 3919-3931.
M. Pushpanathan, P. Gunasekaran, J. Rajendhran, Antimicrobial Peptides: Versatile Biological Properties, Int. J. Pept., 2013, 1-15.
Y. Huan, Q. Kong, H. Mou, H. Yi, Antimicrobial Peptides: Classification, Design, Application and Research Progress in Multiple Fields, Front. Microbiol., 11, 2020, 582779.
J. Xuan, W. Feng, J. Wang, R. Wang, B. Zhang, L. Bo, Z.-S. Chen, H. Yang, L. Sun, Antimicrobial peptides for combating drug-resistant bacterial infections, Drug Resist. Updat, 68, 2023, 100954.
M. Erdem Büyükkiraz, Z. Kesmen, Antimicrobial peptides (AMPs): A promising class of antimicrobial compounds, J. Appl. Microbiol, 132, 2022, 1573-1596.
M. Simmaco, G. Mignogna, S. Canofeni, R. Miele, M.L. Mangoni, D. Barra, Temporins, Antimicrobial Peptides from the European Red Frog Rana temporaria, Eur. J. Biochem, 242, 1996, 788-792.
S.M. Romero, A.B. Cardillo, M.C. Martínez Ceron, S.A. Camperi, S.L. Giudicessi, Temporins: An Approach of Potential Pharmaceutic Candidates, Surg. Infect., 21, 2020, 309-322.
Y. Rosenfeld, D. Barra, M. Simmaco, Y. Shai, M.L. Mangoni, A Synergism between Temporins toward Gram-negative Bacteria Overcomes Resistance Imposed by the Lipopolysaccharide Protective Layer, J. Biol. Chem., 281, 2006, 28565-28574.
C. Avitabile, F. Netti, G. Orefice, M. Palmieri, N. Nocerino, G. Malgieri, L.D. D’Andrea, R. Capparelli, R. Fattorusso, A. Romanelli, Design, structural and functional characterization of a Temporin-1b analog active against Gram-negative bacteria, Biochim. Biophys. Acta BBA - Gen. Subj., 1830, 2013, 3767-3775.
D. Wade, J. Silberring, R. Soliymani, S. Heikkinen, I. Kilpeläinen, H. Lankinen, P. Kuusela, Antibacterial activities of temporin A analogs, FEBS Lett, 479, 2000, 6-9.
R. Ghiselli, A. Giacometti, O. Cirioni, F. Mocchegiani, F. Orlando, W. Kamysz, M.S. Del Prete, J. Lukasiak, G. Scalise, V. Saba, Temporin A as a prophylactic agent against methicillin sodium-susceptible and methicillin sodium-resistant Staphylococcus epidermidis vascular graft infection, J. Vasc. Surg., 36, 2002, 1027-1030.
L. Swithenbank, P. Cox, L.G. Harris, E. Dudley, K. Sinclair, P. Lewis, F. Cappiello, C. Morgan, Temporin A and Bombinin H2 Antimicrobial Peptides Exhibit Selective Cytotoxicity to Lung Cancer Cells, Scientifica, 2020, 1-10.
O. Simonetti, O. Cirioni, G. Goteri, R. Ghiselli, W. Kamysz, E. Kamysz, C. Silvestri, F. Orlando, C. Barucca, A. Scalise, V. Saba, G. Scalise, A. Giacometti, A. Offidani, Temporin A is effective in MRSA-infected wounds through bactericidal activity and acceleration of wound repair in a murine model, Peptides, 29, 2008 520-528.
D. Wade, J.-I. Flock, C. Edlund, I. Lofving-Arvholm, M. Sallberg, T. Bergman, A. Silveira, C. Unson, L. Rollins-Smith, J. Silberring, M. Richardson, P. Kuusela, H. Lankinen, Antibiotic Properties of Novel Synthetic Temporin A Analogs and a Cecropin A-Temporin A Hybrid Peptide, Protein Pept. Lett., 9, 2002, 533-543.
D. Dimitrova, V. Nemska, T. Foteva, I. Iliev, N. Georgieva, D. Danalev, Synthesis and Biological Studies of New Temporin A Analogs Containing Unnatural Amino Acids in Position 7, Pharmaceutics, 16, 2024, 716.
D. Dimitrova, V. Nemska, I. Iliev, S. Petrin, N. Georgieva, D. Danalev, New Temporin A Analogues Modified in Positions 1 and 10—Synthesis and Biological Studies, Pharmaceutics, 17, 2025, 396.
D. Danalev, D. Borisova, S. Yaneva, M. Georgieva, A. Balacheva, T. Dzimbova, I. Iliev, T. Pajpanova, Z. Zaharieva, I. Givechev, E. Naydenova, Synthesis, in vitro biological activity, hydrolytic stability and docking of new analogs of BIM-23052 containing halogenated amino acids, Amino Acids, 52, 2020, 1581-1592.
S. Zhang, M. Ma, Z. Shao, J. Zhang, L. Fu, X. Li, W. Fang, L. Gao, Structure and Formation Mechanism of Antimicrobial Peptides Temporin B- and L-Induced Tubular Membrane Protrusion, Int. J. Mol. Sci., 22, 2021, 11015.
G. Manzo, P.M. Ferguson, V.B. Gustilo, C.K. Hind, M. Clifford, T.T. Bui, A.F. Drake, R.A. Atkinson, J.M. Sutton, G. Batoni, C.D. Lorenz, D.A. Phoenix, A.J. Mason, Minor sequence modifications in temporin B cause drastic changes in antibacterial potency and selectivity by fundamentally altering membrane activity, Sci. Rep., 9, 2019, 1385.
A.C. Rinaldi, M.L. Mangoni, A. Rufo, C. Luzi, D. Barra, H. Zhao, P.K.J. Kinnunen, A. Bozzi, A.D. Giulio, M. Simmaco, Temporin L: antimicrobial, haemolytic and cytotoxic activities, and effects on membrane permeabilization in lipid vesicles, Biochem. J., 368, 2002, 91-100.
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