Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kyoto, Japan.
Zoology Department, Faculty of Science, Al-Azhar University, Assuit, Egypt.
Biosci Biotechnol Biochem. 2021 May 25;85(6):1348-1356. doi: 10.1093/bbb/zbab046.
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.
蜘蛛毒液是一种复杂的生物活性成分混合物，其中肽通过表现出神经毒性或细胞毒性起着重要作用。富含二硫键的肽是毒液的主要成分，但也存在没有二硫键的线性肽，并且通常表现出抗菌活性。在这项研究中，我们使用质谱分析法分析了 Lycosa poonaensis（狼蛛科）蜘蛛的毒液，以寻找新的抗菌肽。结果表明，在 401 种检测到的成分中，有 120 种是非二硫键桥接的肽。从它们中，通过 MS/MS 分析确定了 2 种肽（lyp2370 和 lyp1987）的序列。生物活性测试表明，lyp2370 仅具有微弱的抗菌活性。另一方面，与 Lycosa singoriensi 毒液中的 M-lycotoxin-Ls3b 相同的 lyp1987 表现出显著的抗菌活性。发现 lyp2370 的活性较弱是由于其两亲α螺旋结构的亲水面上存在一个 Glu 残基。
