[Home ] [Archive]   [ فارسی ]  
:: Main :: About :: Current Issue :: Archive :: Search :: Submit :: Contact ::
Main Menu
Home::
Journal Information::
Articles archive::
Publication Ethics::
Peer Review Process::
Indexing Databases::
For Authors::
For Reviewers::
Subscription::
Contact us::
Site Facilities::
::
Google Scholar Metrics

Citation Indices from GS

AllSince 2019
Citations62733583
h-index2719
i10-index18478

..
Search in website

Advanced Search
..
Receive site information
Enter your Email in the following box to receive the site news and information.
..
Registered in

AWT IMAGE

AWT IMAGE

..
:: Volume 29, Issue 4 (10-2021) ::
Journal of Ilam University of Medical Sciences 2021, 29(4): 60-73 Back to browse issues page
Comparison of Antimicrobial Properties and Toxicity of Natural S3 Peptide with Horseshoe Crab Amoebocyte Origin and its Mutants
Sadegh Rezaei1 , Shahin Hadadian * 2, Ramazan ali Khavari nejad1 , Dariush Norouzian3
1- Dept of Biology, Islamic Azad University, Science and Research Branch, Tehran, Iran
2- Dept of Nanotechnology, New Technologies Research Group, Pasteur Institute of Iran, Tehran, Iran , hadadian@yahoo.com
3- Dept of Nanotechnology, New Technologies Research Group, Pasteur Institute of Iran, Tehran, Iran
Abstract:   (1228 Views)
Introduction: Antimicrobial peptides (AMPs) are compounds with antimicrobial properties that are studied widely due to the development of resistance of pathogenic bacteria to antibiotics. In the present study, the toxicity and antimicrobial effects of two natural monomeric peptides (S3 and S∆3) were compared with S3-S∆3 hybrids and S3 tetramers.
Material & Methods: Protein hybrids (S∆3S3-2mer-GS) S3-S∆3 and tetramer protein S3 (S3-4mer-GS) were expressed in E. coli. BL21 (DE3). Following that, the presence of mutant peptides was confirmed, and their antimicrobial activity was compared and evaluated with S3 and S∆3 monomers. Finally, the toxicity of tetramer and hybrid made on the MDA-MB-231 cell line was evaluated and compared.
Findings: The toxicity of the hybrid was slightly increased, compared to the tetramer for eukaryotic cells; however, this increase was negligible at the active concentration of this protein. Cell survival for hybrids was lower for S3 and SΔ3; nonetheless, cell survival for each sequence decreased with increasing time. Furthermore, the inhibition of hybrid microbial growth was improved and compared with tetramer and S3-SΔ3. It was found that an increase in the positive charge of the hybrid protein did not have a toxic effect on the host bacteria.
Discussion & Conclusion: Due to the appropriate expression and increased antimicrobial activity and negligible cytotoxicity, the hybrid peptide S3-S∆3 and tetramer S3 can be considered an effective production strategy to obtain AMPs.
Keywords: Antimicrobial peptides, Factor c, Horseshoe crab, S3-S∆3 protein hybrid, Tetramer S3 peptide
Full-Text [PDF 771 kb]   (455 Downloads)    
Type of Study: Research | Subject: Medical microbiology
Received: 2021/05/4 | Accepted: 2021/09/1 | Published: 2021/11/1
References
1. Zasloff M. Antimicrobial peptides innate immunity and the normally sterile urinary tract. J Am Soc Nephrol2007; 18:2810-6. doi.10.1681/ASN.2007050611
2. Hancock RE, Sahl HG. Antimicrobial and host defense peptides as new anti infective therapeutic strategies. Nat Biotechnol 2006; 24:1551-7. doi.10.1038/nbt1267
3. Guilhelmelli F, Vilela N, Albuquerque P, Derengowski L, Silva I, Kyaw C. Antibiotic development challenges: the various mechanisms of action of antimicrobial peptides and of bacterial resistance. Front Microbiol2013; 4:353. doi.10.3389/fmicb.2013.00353
4. Kotsianidis I, Kokkinou D, Siapati E, Miltiades P, Lamprianidou E. Identification of a chemoresistant oxidative state low leukemic subpopulation in cd34+ human acute myeloid leukemia cell cycle analysis sorted subsets were stained with Ki67. J Stem Cell Res Ther 2014;4:9. doi. 10.4172/2157-7633.100023
5. Li Y. Recombinant production of antimicrobial peptides in Escherichia coli a review. Protein Exp Pur2011; 80:260-7. doi.10.1016/j.pep.2011.08.001
6. Yusupova YR, Skripnikova VS, Kivero AD, Zakataeva NP. Expression and purification of the 5′-nucleotidase YitU from Bacillus species: its enzymatic properties and possible applications in biotechnology. Appl Microbiol Biotechnol2020; 104:2957-72. doi.10.1007/s00253-020-10428-y
7. Rao X, Hu J, Li S, Jin X, Zhang C, Cong Y, et al. Design and expression of peptide antibiotic hpab-β as tandem multimers in Escherichia coli. Peptides2005; 26:721-9. doi. 10.1016/j.peptides.2004.12.016.
8. Leptihn S, Guo L, Frecer V, Ho B, Ding JL, Wohland T. One step at a time: Action mechanism of Sushi1 antimicrobial peptide and derived molecules. Virulence 2010; 1:42-4. doi.10.4161/viru.1.1.10229
9. Chen X, Zaro JL, Shen WC. Fusion proteinlinkers property design and functionality. Adv Drug Deliver Rev2013; 65:1357-69. doi.10.1016/j.addr.2012.09.039
10. Lorenzini DM, Silva JR PI, Fogaça AC, Bulet P, Daffre S. Acanthoscurrin: a novel glycine-rich antimicrobial peptide constitutively expressed in the hemocytes of the spider Acanthoscurria gomesiana. Dev Comp Immunol 2003; 27:781-91. doi.10.1016/s0145-305x(03)00058-2
11. Sperstad SV, Haug T, Vasskog T, Stensvag K. Hyastatin a glycine rich multi domain antimicrobial peptide isolated from the spider crab hemocytes. Mol Immunol 2009; 46:2604-12. doi.10.1016/j.molimm.2009.05.002
12. Zhang SK, Song JW, Gong F, Li SB, Chang HY, Xie HM, et al. Design of an αhelical antimicrobial peptide with improved cell selective and potent anti biofilm activity. Sci Rep2016; 6:27394. doi. 10.1038/srep27394 2016
13. Sepahi M, Ahangari Cohan R, Hadadian S, Norouzian D. Effect of glutamic acid elimination substitution on the biological activities of S3 cationic amphiphilic peptides. Pre Biochem Biotechnol2020; 50:664-72. doi.10.1080/10826068.2020.1725772
14. Yin LM, Edwards MA, Li J, Yip CM, Deber CM. Roles of hydrophobicity and charge distribution of cationic antimicrobial peptides in peptide membrane interactions. J Biol Chem2012; 287:7738-45. doi.10.1074/jbc.M111.303602
15. Shang D, Li X, Sun Y, Wang C, Sun L, Wei S, et al. Design of potent, non-toxic antimicrobial agents based upon the structure of the frog skin peptide temporin1CEb from Chinese brown frog, Rana chensinensis. Chem Biol Drug Des 2012; 79:653-62. doi.10.1111/j.1747-0285.2012.01363.x
16. Baghbeheshti S, Hadadian S, Eidi A, Pishkar L, Rahimi H. Effect of flexible and rigid linkers on biological activity of recombinant tetramer variants of s3 antimicrobial peptide. Int J Pept Res Ther2021; 27:457-62. doi.10.1007/s10989-020-10095-7
17. Gasteiger E, Hoogland C, Gattiker A, Wilkins MR, Appel RD, Bairoch A. Protein identification and analysis tools on the ExPASy server. 2 th ed. Proteom Prot Handbook Totowa New Jersey Springer Publication. 2005; P. 571-607. doi.10.1385/1-59259-890-0:571.
18. Maboudi K, Hosseini SM, Sepahi M, Yaghoubi H, Hadadian S. Production of erythropoietin specific polyclonal antibodies. Iranian J Biotechnol2017; 15:50. doi. doi.org/10.15171/ijb.1413
19. Wiegand I, Hilpert K, Hancock RE. Agar and broth dilution methods to determine the minimal inhibitory concentration of antimicrobial substances. Nat Prot2008; 3:163-75. doi. 10.1038/nprot.2007.521
20. Burns KE, McCleerey TP, Thevenin D. PH selective cytotoxicity of pHLIP antimicrobial peptide conjugates. Sci Rep2016; 6:28465. doi.10.1038/srep28465
21. Cirac A, Torne M, Badosa E, Montesinos E, Salvador P, Feliu L, et al. Rational design of cyclic antimicrobial peptides based on bpc 194 and bpc198. Molecules2017; 22:1054. doi. 10.3390/molecules22071054
22. Almaaytah A, Qaoud MT, Abualhaijaa A, Albalas Q, Alzoubi KH. Hybridization and antibiotic synergism as a tool for reducing the cytotoxicity of antimicrobial peptides. Inf Drug Res2018; 11:835. doi.10.2147/IDR.S166236
23. Ding JL, Ho B. Endotoxin detection from limulus amebocyte lysate to recombinant factor c endotoxins structure. Func Rec Springer Publication.2010. P. 187-208. doi. 10.1007/978-90-481-9078-2_9.
24. Rezaei S, Hadadian S, Khavarinejad RA, Norouzian D. Recombinant tandem repeated expression of s3 and sδ3 antimicrobial peptides. Rep Biochem Mol Biol 2020; 9:348. doi. 10.29252/rbmb.9.3.348
25. Sabourin M, Tuzon CT, Fisher TS, Zakian VA. A flexible protein linker improves the function of epitope tagged proteins in Saccharomyces cerevisiae. Yeast 2007; 24:39-45. doi. 10.1002/yea.1431
26. Li P, Wohland T, Ho B, Ding JL. Perturbation of lipopolysaccharide micelles by sushi 3 antimicrobial peptide the importance of an intermolecular disulfide bond in s3 dimer for binding, disruption, and neutralization of lps. J Biol Chem2004; 279:50150-6. doi. 10.1074/jbc.M405606200
27. Yau YH, Ho B, Tan NS, Ng ML, Ding JL. High therapeutic index of factor C Sushi peptides: potent antimicrobials against Pseudomonas aeruginosa. Antimicrob Age Chemother 2001; 45:2820-5. doi.10.1128/AAC.45.10.2820-2825.2001
28. Conlon JM, Mechkarska M, Arafat K, Attoub S, Sonnevend A. Analogues of the frog skin peptide alyteserin‐2a with enhanced antimicrobial activities against Gram‐negative bacteria. J Pept Sci 2012; 18:270-5. doi.10.1002/psc.2397
29. Dathe M, Nikolenko H, Meyer J, Beyermann M, Bienert M. Optimization of the antimicrobial activity of magainin peptides by modification of charge. FEBS Lett 2001; 501:146-50. doi. 10.1016/S0014-5793(01)02648-5
30. Pal T, Sonnevend A, Galadari S, Conlon JM. Design of potent, non toxic antimicrobial agents based upon the structure of the frog skin peptide pseudin2. Regul Pept 2005; 12 :85-91. doi. 10.1016/j.regpep.2005.01.015
Send email to the article author

Add your comments about this article
Your username or Email:

CAPTCHA



XML   Persian Abstract   Print


Download citation:
BibTeX | RIS | EndNote | Medlars | ProCite | Reference Manager | RefWorks
Send citation to:

Rezaei S, Hadadian S, Khavari nejad R A, Norouzian D. Comparison of Antimicrobial Properties and Toxicity of Natural S3 Peptide with Horseshoe Crab Amoebocyte Origin and its Mutants. J. Ilam Uni. Med. Sci. 2021; 29 (4) :60-73
URL: http://sjimu.medilam.ac.ir/article-1-7080-en.html


Rights and permissions
Creative Commons License This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License.
Volume 29, Issue 4 (10-2021) Back to browse issues page
مجله دانشگاه علوم پزشکی ایلام Journal of Ilam University of Medical Sciences
Persian site map - English site map - Created in 0.15 seconds with 41 queries by YEKTAWEB 4643