Shakiba Darvish Alipour Articles List

List of Articles Shakiba Darvish Alipour

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1 - Anti-biofilm and anti-bacterial effects of bacteriocin-producing strains of Escherichia coli and Bacillus subtilis
Mohammad Reza Sarjoughian Shakiba Darvish Alipour Astaneh
20.1001.1.20083068.1397.11.35.3.7

Background & Objectives: The prevalence of infection, along with the spread of antibiotic-resistant bacteria has caused the antibacterial peptide, bacteriocins, to be considered. The purpose of this study was to compare the antibacterial effect of bacteriocin-produc More

Background & Objectives: The prevalence of infection, along with the spread of antibiotic-resistant bacteria has caused the antibacterial peptide, bacteriocins, to be considered. The purpose of this study was to compare the antibacterial effect of bacteriocin-producing bacteria.Materials & Methods: The inhibitory activity of bacteria isolated from different regions of Semnan soil, Dasht Desert (Semnan University Bacterial Culture Collection; DDBCC) was studied against the indicators by agar diffusion method. Candidate strains were identified by biochemical and molecular tests. Concentrating the selected bacteriocins by ammonium sulfate saturation, the effects of biofilm destruction were studied. Then, using a thin layer chromatography the selected bacteriocins were purified and their antimicrobial activity was confirmed.Results: The 16s rRNA sequencing results showed 98% similarity of DDBCC38 and DDBCC51 isolates to E. coli and 96% similarity of the DDBCC46 isolate to Bacillus subtilis. Concentrated DDBCC51 and DDBCC38 bacteriocins inhibited the growth of Bacillus cereus, Bacillus anthracis, and Klebsiella pneumonia after 52 hours. Pseudomonas aeruginosa and Staphylococcus aureus biofilms were destructed by DDBCC51 and DDBCC38 bacteriocins 12.0% and 40.0%, and 19.6% and 40%, respectively. In contrast, concentrated DDBCC46 bacteriocin was effective on K. pneumonia and P. aeruginosa in 72 hours but had no effect on biofilm destruction. The purification of DDBCC38 and DDBCC51 bacteriocins by thin layer chromatography resulted in 2 mm increasing of inhibition zone diameter against K. pneumoniae. However, purified DDBCC46 bacteriocin reduced it by 4 mm.Conclusion: Considering the anti-biofilm and antagonistic properties of the respective isolates, further studies for optimization of the production conditions and molecular identification of the produced bacteriocin are proposed. Manuscript profile
Open Access Article
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2 - A bioinformatics study of antibacterial peptide Attacin1a in Tenebrio molitor
Mohammad Hossein Karimi Gouraji Mehdi Golestaninasab Shakiba Darvish Alipour
10.30495/jmw.2022.1958619.2020

20.1001.1.20083068.1401.15.0.6.8

Background & Objectives: Nowadays, antimicrobial peptides produced from insects are             considered for their antibacterial activity against pathogens and the fewer side effects. The aim of More

Background & Objectives: Nowadays, antimicrobial peptides produced from insects are             considered for their antibacterial activity against pathogens and the fewer side effects. The aim of this study is a bioinformatics analysis of attacin1a as an antibacterial compound and the             investigation of its physicochemical properties for laboratory research based on the production of drug delivery carriers and vaccine design.Materials & methods: The sequence of attacin1a gene belonged to T. molitor, was extracted in FASTA format from the NCBI database; www.ncbi.nlm.nih.gov. The Molecular weight,            similarity and physicochemical characteristics were investigated in the attacin1a and their          homologous peptides. In addition, the second and tertiary structures of the attacin1a were           predicted using bioinformatics software’s, and the function and immunogenicity of the peptide were studied.Results: Bioinformatics studies showed that the amino acid sequences of the attacin1a were       conserved in the central and c-terminal regions between 10 members of the suborder Polyphaga. The assessment of structural and biochemical properties showed that the attacin1a structure       contains 51% of non-polar amino acids with a disorder index of 61% and flexibility of 53%. The second structure of attacin1a consisted of 52.60% Random coils, 21.43% beta-strands and 21.43% alpha helices. The prediction of the tertiary structure in the Phyre2 showed 32% confidence and 31.1% identity to a beta-immunoglobulin protein (d2aw2a1). This peptide doesn’t have a high ability to stimulate the immune system.Conclusion: The abundance of beta strands in the attacin 1a structure increased the molecule's stability and its ability to cross through the cell membrane in bacteria.  Manuscript profile

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List of Articles Shakiba Darvish Alipour