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首页> 外文期刊>Biochimica et biophysica acta: BBA: International journal of biochemistry, biophysics and molecular biololgy. Proteins and Proteomics >Identification and structural analysis of the antimicrobial domain in hipposin, a 51-mer antimicrobial peptide isolated from Atlantic halibut
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Identification and structural analysis of the antimicrobial domain in hipposin, a 51-mer antimicrobial peptide isolated from Atlantic halibut

机译：鉴定和结构分析的河马素中的抗菌域，一种从大西洋大比目鱼中分离出来的51-mer抗菌肽

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摘要

Hipposin is a potent 51-mer antimicrobial peptide (AMP) from Atlantic halibut with sequence similarity to parasin (19-mer catfish AMP), buforin I (39-mer toad AMP), and buforin II (an active 21-mer fragment of buforin I), suggesting that the antimicrobial activity of these peptides might all be due to a common antimicrobial sequence motif. In order to identify the putative sequence motif, the antimicrobial activity of hipposin fragments against 20 different bacteria was compared to the activity of hipposin, parasin and buforin II. Neither parasin nor the 19-mer parasin-like fragment HIP(1–19) (differs from parasin in only three residues) that is derived from the N-terminal part (residues 1–19) of hipposin had marked antimicrobial activity. In contrast, the fragment HIP(16–36) (identical to buforin II) that is derived from the middle part of hipposin (residues 16–36) had such activity, indicating that this part of hipposin contained an antimicrobial sequence motif. The activity was enhanced when the parasin-like N-terminal sequence was also present, as the fragment HIP(1–36) which consists of residues 1–36 in hipposin was more potent than HIP(16–36). Extending HIP(1–36) with three C-terminal residues—thereby constructing the buforin I-like peptide HIP(1–39) (differs from buforin I in only three residues)—increased the activity further. Also, the presence of the C-terminal part of hipposin (residues 40–51) increased the activity, as hipposin was clearly the most potent of all the peptides that were tested. Circular dichroism structural analysis of the peptides revealed that they were all non-structured in aqueous solution. However, trifluoroethanol and the membrane-mimicking entities dodecylphosphocholine micelles and negatively charged liposomes induced (amphiphilic) α-helical structuring in hipposin. Judging from the structuring of the individual fragments, the tendency for α-helical structuring appeared to be greater in the C-terminal and the buforin II-like middle region of hipposin than in the parasin-like N-terminal region.
机译：Hipposin是一种来自大西洋大比目鱼的强效51-mer抗菌肽（AMP），其序列与parasin（19-mer fish鱼AMP），buforin I（39-merad AMP）和buforin II（buforin的21mer活性片段）相似I），表明这些肽的抗微生物活性可能全部归因于共同的抗微生物序列基序。为了鉴定推测的序列基序，将河马蛋白片段对20种不同细菌的抗菌活性与河马蛋白，parasin和buforin II的活性进行了比较。源自河马蛋白N末端部分（残基1-19）的parasin或19-mer parasin样片段HIP（1-19）（与parasin仅有三个残基不同）都没有显着的抗菌活性。相反，源自河马蛋白中部（残基16-36）的片段HIP（16-36）（与buforin II相同）具有这种活性，表明该河马蛋白的这一部分含有抗菌序列基序。当还存在parasin-like N-末端序列时，活性增强，因为由Hipposin中的1-36位残基组成的HIP（1-36）片段比HIP（16-36）更有效。用三个C末端残基扩展HIP（1-36），从而构建类似buforin I的肽HIP（1-39）（与buforin I的区别仅三个残基），从而进一步提高了活性。另外，河马蛋白C末端部分（残基40-51）的存在增加了活性，因为河马蛋白显然是所有测试肽中最有效的。肽的圆二色性结构分析表明，它们在水溶液中都是非结构化的。然而，三氟乙醇和模仿膜的实体十二烷基磷酸胆碱胶束和带负电荷的脂质体在河马蛋白中诱导了（两亲性）α-螺旋结构。从单个片段的结构来看，α-螺旋结构的趋势似乎在河马蛋白的C末端和buforin II样中间区域比在parasin样N末端区域更大。

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