[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
Citations62753585
h-index2719
i10-index18578

..
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): 103-116 Back to browse issues page
Evaluation of the Effect of Less Negatively Charged Amino Acid Substitution in Synthetic Tetramer Peptide S3 Derived from Horseshoe Crab Ambocyte on its Antibacterial Properties
Sakineh Baghbeheshti1 , Shahin Hadadian * 2, Akram Eidi1 , Leila Pishkar3 , Hamzeh Rahimi4
1- Dept of Biology, Islamic Azad University, Science and Research Branch, Tehran, Iran
2- Dept of Nanotechnology, Dept of New Technologies Research, Pasteur Institute of Iran, Tehran, Iran , hadadian@yahoo.com
3- Dept of Biology, Faculty of Sciences, Islamic Azad University, Islamshahr Branch, Islamshahr, Iran
4- Dept of Molecular Medicine, New Technologies Research Group, Pasteur Institute of Iran, Tehran, Iran
Abstract:   (1377 Views)
Introduction: The study of the effects of synthetic peptides with antibacterial properties can provide more effective antibiotics. This study designed, expressed, and investigated the Sushi 3 tetramer peptide. Subsequently, it was compared in terms of changing antibacterial properties with another Sushi3 tetramer peptide the aspartic acid and proline amino acids of which were replaced with glycine and serine amino acids.
Material & Methods: First, the mentioned Sushi3 tetramer peptide sequences were designed, constructed, and named Mer1 and Mer 2, respectively, and cloned separately into plasmid pET-26b (+) and finally transferred to E.coli BL21 host (DE3). After the expression of the peptides, the presence of peptides was confirmed by SDS-PAGE and Western blotting. Afterward, the antimicrobial activity of Mer1 and Mer 2 was evaluated and compared. Finally, the toxicity of the two tetramers made on the MDA-MB-231 cell line was evaluated and compared.
Findings: Mer1 and Mer 2 had similar protein expression, and the toxic effect of both peptides on the cell line was not significantly different. however, Mer 2 had more effective antimicrobial effects than Mer1 at the same concentrations.
Discussion & Conclusion: Evaluation of the effect of amino acid replacement with less negatively charge on increasing the antimicrobial activity of peptides is a suitable strategy. The above results increase the possibility of designing and producing antimicrobial peptides against antibiotic-resistant strains as the next generation of antibiotics.
Keywords: Antimicrobial peptides, Factor c, Horseshoe crab, Sushi3 tetramer peptide
Full-Text [PDF 795 kb]   (634 Downloads)    
Type of Study: Research | Subject: clinical biochemistry
Received: 2021/04/3 | Accepted: 2021/06/27 | Published: 2021/11/1
References
1. Kaye KS, Pogue JM. Infections Caused by Resistant Gram‐Negative Bacteria: Epidemiology and Management. Pharmacotherapy: The Journal of Human Pharmacology and Drug Therapy. 2015;35:949-62. doi.10.1002/phar.1636.
2. Jenkinez V, Ranjitha K. Phytochemical and antibacterial studies of chicory a multipurpose medicinal plant stress physiology and medicinal plant biotechnology unit. Sch Life Sci Bharathidasan Uni Nadu India2008;2:620 4.
3. Moniri R, Mosayebi Z, Movahedian AH, Mossavi GhA. Increasing trend of antimicrobial drug-resistance in Pseudomonas aeruginosa causing septicemia. Iranian J Pub Health 2006;35:58-62.
4. Evelien Berends. Role of antimicrobial peptides in human innate defense against bacteria master program Infection and Immunity. Msc Thes Uni Med Cent Utrech Heidelberglaan2010;1-70.
5. Guilhelmell N, Vilel F. 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.
6. Engler AC, Wiradharma N, Ong ZY, Coady DJ, Hedrick JL, Yang YY. Emerging trends in macromolecular antimicrobials to fight multi drug resistant infections. Nan Tod2012;7:201-22. doi. 10.1016/j.nantod.2012.04.003.
7. Maisetta G, Grassi L, Di Luca M, Bombardelli S, Medici C, Brancatisano FL, et al. Anti biofilm properties of the antimicrobial peptide temporin 1Tb and its ability, in combination with EDTA, to eradicate Staphylococcus epidermidis biofilms on silicone catheters. Biofouling 2016;32 :787-800. doi. 10.1080/08927014.2016.1194401.
8. Mansour SC, Hancock RE. Peptide idr1018 modulating the immune system and targeting bacterial biofilms to treat antibioticresistant bacterial infections. J Pept Sci 2015;21:323-9. doi. 10.1002/psc.2708.
9. 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.
10. Ding J L, Ho B. inventors; Google Patents, assignee. Sushi peptide multimer patent. 2010;US7763704B2.
11. Leptihn S, Guo L, Frecer V, Ho B, Ding J L, 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.
12. Asoodeh A, Zardini H Z, J C. Identification and characterization of two novel antimicrobial peptides, temporin‐Ra and temporin Rb from skin secretions of the marsh frog rana ridibunda. J Pept Sci2012; 18:10-6. doi.10.1002/psc.1409.
13. Přistoupil TI, Kramlova M, Štěrbíková J. On the mechanism of adsorption of proteins to nitrocellulose in membrane chromatography. J Chromatograph1969; 42:367-75. doi.10.1016/S0021-9673(01)80636-1.
14. Tang RH, Li M, Liu LN, Zhang SF, Alam N, You M, Ni YH, Li ZD. Chitosan modified nitrocellulose membrane for paper based point of care testing. Cellulose2020;27:3835-46. doi.10.1007/s10570-020-03031-x.
15. Wiegand I, Hilpert K, Hancock RE. Agar and broth dilution methods to determine the minimal inhibitory concentration of antimicrobial substances. Nature Prot 2008 ;3:163-75. doi. 10.1038/nprot.2007.521.
16. Markossian S, Grossman A, Brimacombe K, Arkin M, Auld D, Austin CP, et al. Assay guidance manual bethesda. 1th ed. Comp National Cent Adv Trans Sci Publication. 2004;P.33-86.
17. Ding JL, Li P, Ho B. The Sushi peptides structural characterization and mode of action against Gram negative bacteria. Cell Mol Life Sci2008;65:1202-19. doi.10.1007/s00018-008-7456-0.
18. 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. Virulence2010;1:42-4. doi. 10.4161/viru.1.1.10229.
19. Leptihn S, Har JY, Chen J, Ho B, Wohland T, Ding JL. Single molecule resolution of the antimicrobial action of quantum dot labeled sushi peptide on live bacteria. BMC Biolo 2009;7:1-3. doi.10.1186/1741-7007-7-22 .
20. Li P, Sun M, Wohland T, Ho B, Ding JL. The molecular mechanism of interaction between sushi peptide and Pseudomonas endotoxin. Cell Mol Immunol2006;3:21-8.
21. Ding JL, Zhu Y, Ho B. High-performance affinity capture removal of bacterial pyrogen from solutions. J Chromatograph Biomed Sci Appl 2001;759:237-46. doi.10.1016/S0378-4347(01)00227-4.
22. Ding J, Ho B, Tan N, inventors. Recombinant proteins and peptides for endotoxin biosensors endotoxin removal and anti microbial and anti endotoxin. Therapeutics2003;3:213-8.
23. 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 Rep 2016;6:1-3. doi.10.1038/srep27394.
24. Lee M, Bang K, Kwon H, Cho S. Enhanced antibacterial activity of an attacin-coleoptericin hybrid protein fused with a helical linker. Mole Biol Rep 2013;40:3953-60. doi.10.1007/s11033-012-2472-4
25. Lorenzini DM, Silva JRPI, Fogaça AC, Bulet P, Daffre S. Acanthoscurrin a novel glycine rich antimicrobial peptide constitutively expressed in the hemocytes of the spider acanthoscurria gomesiana. Deve Comp Immunol2018 ;27:781-91. doi.10.1016/S0145-305X(03)00058-2.
26. Park CJ, Park CB, Hong SS, Lee HS, Lee SY, Kim SC. Characterization and cDNA cloning of two glycine and histidine-rich antimicrobial peptides from the roots of shepherd's purse Capsella bursa pastoris. Plant Mole Biol2000;44:187-97. doi:10.1023/a:1006431320677.
27. Sperstad SV, Haug T, Vasskog T, Stensvåg K. Hyastatin, a glycine-rich multi-domain antimicrobial peptide isolated from the spider crab (Hyas araneus) hemocytes. Molecular Immunology. 2009 Aug 1;46(13):2604-12. doi: [DOI:10.1016/j.molimm.2009.05.002.]
28. Ding JL, Ho B. Inventors assignee sushi peptides. 1 th ed. Multimer Publication. 2005;P.245-66.
29. Ding JL, Ho B, Inventors assignee sushi peptides. 3th ed. Multimer Publication. 2010;P.133-72.
30. 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. Peptides 2005;26:721-9. doi. 10.1016/j.peptides.2004.12.016
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:

Baghbeheshti S, Hadadian S, Eidi A, Pishkar L, Rahimi H. Evaluation of the Effect of Less Negatively Charged Amino Acid Substitution in Synthetic Tetramer Peptide S3 Derived from Horseshoe Crab Ambocyte on its Antibacterial Properties. J. Ilam Uni. Med. Sci. 2021; 29 (4) :103-116
URL: http://sjimu.medilam.ac.ir/article-1-7050-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