Discovery of new marine biopharmaceutics, via proteomics
Discovery of new marine biopharmaceutics, via proteomics
Naghmeh Roohi-Shalmaee,1Rezvan Mousavi Nadushan,2,*
1. Department of Marine Science, Faculty of Natural Resources and Environment, Science and Research Branch, Islamic Azad University, Tehran, Iran. 2. Department of Marine Science, Faculty of Natural Resources and Environment, Tehran North Branch, Islamic Azad University Tehran, Iran.
Introduction: At the moment, according to antibiotics resistance, finding new effective biopharmaceuticals seems unavoidable. So in this critical condition, antimicrobial proteome extracted from natural sources can be useful to overcome this challenge. So diverse kinds of organisms like marine organisms has been investigated for their immunological responses to find antimicrobial agents. Serpulids of the Persian Gulf are one of these organisms that we focused on it to find antibacterial peptides or proteins.
Methods: Accordingly, at first HPLC-purified fractions of the coelomic fluid of these organisms were collected and then antibacterial activities of HPLC-purified fractions were investigated against gram negative/positive bacteria, and were assessed by inhibitory kinetic assay, two HPLC-purified fractions; F11, and FPIXC, showed antibacterial activity against gram-negative bacteria. The nature of purified fractions, F11 was defined as protein band at MW of ca. 65 kDa but F23 demonstrated a heterogeneous character. Subsequently, the proteinous fraction of major fraction, F23, was isolated by anion exchange chromatography as FPIXC. Hemolysis and MTT assays were performed on Human Embryonic Kidney 293 (HEK-293) cells, to investigate in vitro toxicity of F11 and FPIXC. Then characterizations of candidates were followed by MALDI-TOF analyses for partial identification. Bioinformatics analyses were subsequently employed to find their homologs, also used for determining their roles.
Results: The antibacterial activity of F11 was estimated to be twofold of FPIXC against Aeromonas hydrophila and Escherichia coli. F11 and FPIXC demonstrated similar activities on Vibrio harveyi, and no activity on Staphylococcus aureus. The MW of FPIXC was 8.5 kDa also it was distinguished as a unique peptide. F11 as one of the qualitatively dominant pure proteinous fractions showed homology with albumin protein.
Conclusion: Finally, two low toxic antibacterial proteome including homologs of the albumin and one unique peptide, were explored as possible new antibiotic in medical microbiology.