List of Articles پپتید ضد باکتریایی

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  1 - 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
  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