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Paralithocins, Antimicrobial Peptides with Unusual Disulfide Connectivity from the Red King Crab, Paralithodes camtschaticus
Journal of Natural Products ( IF 3.3 ) Pub Date : 2018-01-17 00:00:00 , DOI: 10.1021/acs.jnatprod.7b00780 Morten K. Moe 1 , Tor Haug 2 , Magne O. Sydnes 3, 4 , Sigmund V. Sperstad 2 , Chun Li 2 , Lena C. Vaagsfjord 2 , Enrique de la Vega 5 , Klara Stensvåg 2, 5
Journal of Natural Products ( IF 3.3 ) Pub Date : 2018-01-17 00:00:00 , DOI: 10.1021/acs.jnatprod.7b00780 Morten K. Moe 1 , Tor Haug 2 , Magne O. Sydnes 3, 4 , Sigmund V. Sperstad 2 , Chun Li 2 , Lena C. Vaagsfjord 2 , Enrique de la Vega 5 , Klara Stensvåg 2, 5
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As part of an ongoing exploration of marine invertebrates as a source of new antimicrobial peptides, hemocyte extracts from the red king crab, Paralithodes camtschaticus, were studied. Three cationic cysteine (Cys)-rich peptides, named paralithocins 1–3, were isolated by bioassay-guided purification, and their amino acid sequences determined by Edman degradation and expressed sequences tag analysis. Disulfide bond mapping was performed by high-resolution tandem mass spectrometry. The peptides (38–51 amino acids in length) share a unique Cys motif composed of eight Cys, forming four disulfide bridges with a bond connectivity of (Cys relative position) Cys1–Cys8, Cys2–Cys6, Cys3–Cys5, and Cys4–Cys7, a disulfide arrangement that has not been previously reported among antimicrobial peptides. Thus, paralithocins 1–3 may be assigned to a previously unknown family of antimicrobial peptides within the group of Cys-rich antimicrobial peptides. Although none of the isolated peptides displayed antimicrobial activity against the target strains Escherichia coli, Pseudomonas aeruginosa, or Staphylococcus aureus, they inhibited the growth of several marine bacterial strains with minimal inhibitory concentrations in the 12.5–100 μM range. These findings corroborate the hypothesis that marine organisms are a valuable source for discovering bioactive peptides with new structural motifs.
中文翻译：
Paralithocins，来自红色帝王蟹，Paralithodes camtschaticus的具有不寻常的二硫键连接性的抗菌肽
作为对海洋无脊椎动物作为新抗菌肽来源的一项持续探索的一部分，红帝王蟹（Paralithodes camtschaticus）的血细胞提取物，进行了研究。通过生物测定指导纯化分离了三种富含阳离子半胱氨酸（Cys）的肽，称为顺石霉素1-3，并通过Edman降解和表达序列标签分析确定了其氨基酸序列。二硫键映射通过高分辨率串联质谱进行。肽段（长度为38-51个氨基酸）共有一个由8个半胱氨酸组成的独特半胱氨酸基序，形成四个二硫键，并具有（半胱氨酸相对位置）半胱氨酸-半胱氨酸8，半胱氨酸2-半胱氨酸6，半胱氨酸3-半胱氨酸5和半胱氨酸4- Cys7，一种二硫键排列，以前未在抗菌肽中报道过。因此，在富含Cys的抗菌肽组中，副石蜡1–3可能被分配给以前未知的抗菌肽家族。大肠杆菌，铜绿假单胞菌或金黄色葡萄球菌，它们以12.5–100μM的最小抑制浓度抑制了几种海洋细菌菌株的生长。这些发现证实了以下假设：海洋生物是发现具有新结构基序的生物活性肽的宝贵来源。
更新日期：2018-01-17
中文翻译：
Paralithocins，来自红色帝王蟹，Paralithodes camtschaticus的具有不寻常的二硫键连接性的抗菌肽
作为对海洋无脊椎动物作为新抗菌肽来源的一项持续探索的一部分，红帝王蟹（Paralithodes camtschaticus）的血细胞提取物，进行了研究。通过生物测定指导纯化分离了三种富含阳离子半胱氨酸（Cys）的肽，称为顺石霉素1-3，并通过Edman降解和表达序列标签分析确定了其氨基酸序列。二硫键映射通过高分辨率串联质谱进行。肽段（长度为38-51个氨基酸）共有一个由8个半胱氨酸组成的独特半胱氨酸基序，形成四个二硫键，并具有（半胱氨酸相对位置）半胱氨酸-半胱氨酸8，半胱氨酸2-半胱氨酸6，半胱氨酸3-半胱氨酸5和半胱氨酸4- Cys7，一种二硫键排列，以前未在抗菌肽中报道过。因此，在富含Cys的抗菌肽组中，副石蜡1–3可能被分配给以前未知的抗菌肽家族。大肠杆菌，铜绿假单胞菌或金黄色葡萄球菌，它们以12.5–100μM的最小抑制浓度抑制了几种海洋细菌菌株的生长。这些发现证实了以下假设：海洋生物是发现具有新结构基序的生物活性肽的宝贵来源。
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