DOI: 10.18413/2658-6533-2024-10-2-0-6

In vitro activity of the novel antimicrobial peptide WR-286 in combination with vancomycin against methicillin-resistant
Staphylococcus aureus

Background: Multidrug resistance bacteria are a serious problem for health specialists and all the people in the world. The main reasons for this problem are the misuse of antibiotics and the limited number of antibiotics as compared to different human diseases. The important antibiotic-resistant bacteria include Methicillin-resistant Staphylococcus aureus (MRSA). Antimicrobial peptides (AMPs) are regarded as promising antimicrobial agents because they satisfy the requirements for the creation of innovative antimicrobial drugs. The aim of the study:To design a novel antimicrobial peptide and study its effect against MRSA when we combined it with vancomycin. Materials and methods: To produce the hexapeptide WR-286, 1-(2, 6-difluorobenzyl)-1H-1, 2, 3-triazole-4-carboxylic acid, tryptophan (W), and arginine (R) were rationally combined. Different bacterial strains were used to test WR-286's antibacterial properties. Investigations of WR-286's hemolytic activity toward human erythrocytes were also conducted. Finally, utilizing the checkerboard approach and the fractional inhibitory index, synergistic tests with vancomycin were carried out. Results: With MIC values as low as 35 μM, WR-286 demonstrated strong antibacterial activity against MRSA. The toxicity of WR-286 to human red blood cells was very low. Additionally, the peptide and vancomycin's activity were improved by the synergistic experiments. Conclusion: According to the current investigation, WR-286 has little hemolytic activity and displays promising antibacterial activity against MRSA. Additionally, when coupled with vancomycin, the peptide has synergistic effect. The novel AMPs described in this work are promising potential candidates for antimicrobial drug development

Keywords: antimicrobial peptide, WR-286, minimum inhibitory concentration, MRSA, vancomycin, antibiotic resistance.

Number of views: 379 (view statistics)

Количество скачиваний: 534

Full text (HTML)Full text (PDF)To articles list

Information for citation:

Salama AH. In vitro activity of the novel antimicrobial peptide WR-286 in combination
with vancomycin against methicillin-resistant Staphylococcus aureus. Research Results in Biomedicine.
2024;10(2):244-251. DOI: 10.18413/2658-6533-2024-10-2-0-6

User comments
Reference lists

While nobody left any comments to this publication.
You can be first.

Ahmed A, Siman-Tov G, Hall G, et al. Human antimicrobial peptides as therapeutics for viral infections. Viruses. 2019;11(8):704. DOI: https://doi.org/10.3390/v11080704
Ahn M, Gunasekaran P, Rajasekaran G, et al. Pyrazole derived ultra-short antimicrobial peptidomimetics with potent anti-biofilm activity. European Journal of Medicinal Chemistry. 2017;125:551-564. DOI: https://doi.org/10.1016/j.ejmech.2016.09.071
Avci FG, Akbulut BS, Ozkirimli E. Membrane active peptides and their biophysical characterization. Biomolecules. 2018;8(3):77. DOI: https://doi.org/10.3390/biom8030077
Baeriswyl S, Gan BH, Siriwardena TN, et al. X-ray crystal structures of short antimicrobial peptides as Pseudomonas aeruginosa Lectin B complexes. ACS Chemical Biology. 2019;14(4):758-766. DOI: https://doi.org/10.1021/acschembio.9b00047
Bakka TA, Strøm MB, Andersen JH, et al. Methyl propiolate and 3-butynone: Starting points for synthesis of amphiphilic 1, 2, 3-triazole peptidomimetics for antimicrobial evaluation. Bioorganic and Medicinal Chemistry. 2017;25(20):5380-5395. DOI: https://doi.org/10.1016/j.bmc.2017.07.060
Bártová V, Bárta J, Jarošová M. Antifungal and antimicrobial proteins and peptides of potato (Solanum tuberosum L.) tubers and their applications. Applied Microbiology and Biotechnology. 2019;103(14):5533-5547. DOI: https://doi.org/10.1007/s00253-019-09887-9
Bassetti M, Carnelutti A, Peghin M. Patient specific risk stratification for antimicrobial resistance and possible treatment strategies in gram-negative bacterial infections. Expert Review of Anti-Infective Therapy. 2017;15(1):55-65. DOI: https://doi.org/10.1080/14787210.2017.1251840
Bassetti M, Giacobbe DR. A look at the clinical, economic, and societal impact of antimicrobial resistance in 2020. Expert Opinion on Pharmacotherapy. 2020;21(17):2067-2071. DOI: https://doi.org/10.1080/14656566.2020.1802427
Floch V, Loisel S, Guenin E, et al. Cation substitution in cationic phosphonolipids: a new concept to improve transfection activity and decrease cellular toxicity. Journal of Medicinal Chemistry. 2020;43(24):4617-4628. DOI: https://doi.org/10.1021/jm000006z
Han X, Zheng J, Lin F, et al. Interactions between surface-immobilized antimicrobial peptides and model bacterial cell membranes. Langmuir. 2018;34(1):512-520. DOI: https://doi.org/10.1021/acs.langmuir.7b03411
Haug BE, Camilio KA, Eliassen LT, et al. Discovery of a 9-mer cationic peptide (LTX-315) as a potential first in class oncolytic peptide. Journal of Medicinal Chemistry. 2016;59(7):2918-2927. DOI: https://doi.org/10.1021/acs.jmedchem.5b02025
Hazam PK, Goyal R, Ramakrishnan V. Peptide based antimicrobials: design strategies and therapeutic potential. Progress in Biophysics and Molecular Biology. 2019;142:10-22. DOI: https://doi.org/10.1016/j.pbiomolbio.2018.08.006
Kang SJ, Park SJ, Mishig-Ochir T, et al. Antimicrobial peptides: therapeutic potentials. Expert Review of Anti-Infective Therapy. 2014;12(12):1477-1486. DOI: https://doi.org/10.1586/14787210.2014.976613
Kern AD, Oliveira MA, Coffino P, et al. Structure of mammalian ornithine decarboxylase at 1.6 Å resolution: stereochemical implications of PLP-dependent amino acid decarboxylases. Structure. 1999;7(5):567-581. DOI: https://doi.org/10.1016/S0969-2126(99)80073-2
Kiprono GK. Medication Related Problems Among Patients On Antibiotic Therapy In The Medical Wards At Kenyatta National Hospital--University Of Nairobi. University of Nairobi; 2019.
Kumar P, Kizhakkedathu JN, Straus SK. Antimicrobial peptides: diversity, mechanism of action and strategies to improve the activity and biocompatibility in vivo. Biomolecules. 2018;8(1):4. DOI: https://doi.org/10.3390/biom8010004
Lau QY, Ng FM, Cheong JWD, et al. Discovery of an ultra-short linear antibacterial tetrapeptide with anti-MRSA activity from a structure–activity relationship study. European Journal of Medicinal Chemistry. 2015;105:138-144. DOI: https://doi.org/10.1016/j.ejmech.2015.10.015
Laverty G, McLaughlin M, Shaw C, et al. Antimicrobial activity of short, synthetic cationic lipopeptides. Chemical Biology and Drug Design. 2010;75(6):563-569. DOI: https://doi.org/10.1111/j.1747-0285.2010.00973.x
Lee AS, de Lencastre H, Garau J, et al. Methicillin-resistant Staphylococcus aureus. Nature Reviews Disease Primers. 2018;4:18033. DOI: https://doi.org/10.1038/nrdp.2018.33
Lewies A, Du Plessis LH, Wentzel JF. Antimicrobial peptides: the Achilles’ heel of antibiotic resistance? Probiotics and Antimicrobial Proteins. 2019;11(2):370-381. DOI: https://doi.org/10.1007/s12602-018-9465-0
Li Y, Xiang Q, Zhang Q, et al. Overview on the recent study of antimicrobial peptides: origins, functions, relative mechanisms and application. Peptides. 2012;37(2):207-215. DOI: https://doi.org/10.1016/j.peptides.2012.07.001
Mylonakis E, Podsiadlowski L, Muhammed M, et al. Diversity, evolution and medical applications of insect antimicrobial peptides. Philosophical Transactions of the Royal Society B: Biological Sciences. 2016;371(1695):20150290. DOI: https://doi.org/10.1098/rstb.2015.0290
Nuti R, Goud NS, Saraswati AP, et al. Antimicrobial peptides: a promising therapeutic strategy in tackling antimicrobial resistance. Current Medicinal Chemistry. 2017;24(38):4303-4314. DOI: https://doi.org/10.2174/0929867324666170815102441
Oddo A, Hansen PR. Hemolytic activity of antimicrobial peptides. In: Hansen PR, editor. Antimicrobial Peptides. Springer; 2017. DOI: http://dx.doi.org/10.1007/978-1-4939-6737-7_32
Pandey BK, Srivastava S, Singh M, et al. Inducing toxicity by introducing a leucine-zipper-like motif in frog antimicrobial peptide, magainin 2. Biochemical Journal. 2011;436(3):609-620. DOI: https://doi.org/10.1042/BJ20110056
Pasupuleti M, Schmidtchen A, Malmsten M. Antimicrobial peptides: key components of the innate immune system. Critical Reviews in Biotechnology. 2012;32(2):143-171. DOI: https://doi.org/10.3109/07388551.2011.594423
Patel S, Preuss CV, Bernice F. Vancomycin in: StatPearls. StatPearls Publishing, Treasure Island (FL); 2020.
Pletzer D, Hancock REW. Antibiofilm peptides: potential as broad-spectrum agents. Journal of Bacteriology. 2016;198(19):2572-2578. DOI: https://doi.org/10.1128/jb.00017-16
Rajchakit U, Sarojini V. Recent developments in antimicrobial-peptide-conjugated gold nanoparticles. Bioconjugate Chemistry. 2017;28(11):2673-2686. DOI: https://doi.org/10.1021/acs.bioconjchem.7b00368
Rodríguez-Bano J, Navarro MD, Romero L, et al. Epidemiology and clinical features of infections caused by extended-spectrum beta-lactamase-producing Escherichia coli in nonhospitalized patients. Journal of Clinical Microbiology. 2004;42(3):1089-1094. DOI: https://doi.org/10.1128/jcm.42.3.1089-1094.2004
Rodriguez LMDL, Hemar Y, Cornish J, et al. Structure–mechanical property correlations of hydrogel forming β-sheet peptides. Chemical Society Reviews. 2016;45(17):4797-4824. DOI: https://doi.org/10.1039/C5CS00941C
Rončević T, Vukičević D, Ilić N, et al. Antibacterial activity affected by the conformational flexibility in glycine–lysine based α-helical antimicrobial peptides. Journal of Medicinal Chemistry. 2018;61(7):2924-2936. DOI: https://doi.org/10.1021/acs.jmedchem.7b01831
Rosenthal VD, Maki DG, Jamulitrat S, et al. International nosocomial infection control consortium (INICC) report, data summary for 2003-2008, issued June 2009. American Journal of Infection Control. 2010;38(2):95-104.e2. DOI: https://doi.org/10.1016/j.ajic.2009.12.004
Roudi R, Syn NL, Roudbary M. Antimicrobial peptides as biologic and immunotherapeutic agents against cancer: a comprehensive overview. Frontiers in Immunology. 2017;8:1320. DOI: https://doi.org/10.3389/fimmu.2017.01320
Svendsen JSM, Grant TM, Rennison D, et al. Very short and stable lactoferricin-derived antimicrobial peptides: design principles and potential uses. Accounts of Chemical Research. 2019;52(3):749-759. DOI: https://doi.org/10.1021/acs.accounts.8b00624
Takemori N, Ooi HK, Imai G, et al. Possible mechanisms of action of clarithromycin and its clinical application as a repurposing drug for treating multiple myeloma. Ecancermedicalscience. 2020;14:1088. DOI: https://doi.org/10.3332/ecancer.2020.1088

All journals

Send article

Research Results in Biomedicine is included in the scientific database of the RINTs (license agreement No. 765-12/2014 dated 08.12.2014).

The journal is included in the list of peer-reviewed scientific publications recommended by the Higher Attestation Commission

The journal is indexed by the following scientific databases and platforms

Research Results in Biomedicine (ISSN 2658-6533)

The journal materials and website are licensed under Creative Commons «Attribution» 4.0 International.

The Founder: Federal State Autonomous Educational Institution of Higher Education "Belgorod National Research University"The Founder’s address: 85 Pobedy Street, Belgorod, the Belgorod region, 308015, Russia

The Publisher: Federal State Autonomous Educational Institution of HigherEducation "Belgorod National Research University" The Founder’s address:85 Pobedy Street, Belgorod, the Belgorod region, 308015, Russia

Editors Office: chief editor Mikhail I. Churnosov, e-mail: RR_MedPharm@bsu.edu.ru, phone: +7 (4722) 30-14-03.

Regulations on the Journal

Certificate

Have questions?
You can write to us:

✉ Content manager

✉ Site administration

✉ Executive Secretary

Research Results in Biomedicine

In vitro activity of the novel antimicrobial peptide WR-286 in combination with vancomycin against methicillin-resistantStaphylococcus aureus

The journal is indexed by the following scientific databases and platforms

In vitro activity of the novel antimicrobial peptide WR-286 in combination with vancomycin against methicillin-resistant
Staphylococcus aureus