Characterization of 2 linear peptides without disulfide bridges from the venom of the spider Lycosa poonaensis (Lycosidae)
| Autor: | Masahiro Miyashita, Yusuke Yoshimoto, Mohammed Abdel-Wahab, Yoshiaki Nakagawa, Alhussin M A Megaly, Hisashi Miyagawa, Yugo Tsunoda |
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| Rok vydání: | 2021 |
| Předmět: |
Protein Conformation
alpha-Helical 0301 basic medicine Antimicrobial peptides Spider Venoms Venom complex mixtures Applied Microbiology and Biotechnology Biochemistry Analytical Chemistry 03 medical and health sciences Tandem Mass Spectrometry Animals Amino Acid Sequence Cytotoxicity Molecular Biology Spider 030102 biochemistry & molecular biology biology Chemistry Organic Chemistry Spiders Biological activity General Medicine biology.organism_classification Antimicrobial 030104 developmental biology Antibacterial activity Hydrophobic and Hydrophilic Interactions Lycosa Antimicrobial Cationic Peptides Biotechnology |
| Zdroj: | Bioscience, Biotechnology, and Biochemistry. 85:1348-1356 |
| ISSN: | 1347-6947 |
| DOI: | 10.1093/bbb/zbab046 |
| Popis: | Spider venom is a complex mixture of bioactive components, in which peptides play an important role by showing neurotoxicity or cytotoxicity. Disulfide-rich peptides are major components in the venom, but linear peptides without disulfide bridges are also present and often show antimicrobial activity. In this study, we analyzed the venom of the spider Lycosa poonaensis (Lycosidae) to find novel antimicrobial peptides using mass spectrometry. The result revealed that 120 out of 401 detected components were nondisulfide-bridged peptides. From them, the sequence of 2 peptides (lyp2370 and lyp1987) were determined by MS/MS analysis. The biological activity test revealed that lyp2370 has only weak antibacterial activity. On the other hand, lyp1987, which is identical to M-lycotoxin-Ls3b from the Lycosa singoriensi venom, showed significant antibacterial activity. The weak activity of lyp2370 was found to be due to the presence of a Glu residue on the hydrophilic face of its amphipathic α-helical structure. |
| Databáze: | OpenAIRE |
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