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首页> 外文期刊>Biochemistry >Lytic Activity and Structural Differences of Amphipathic Peptides Derived from Trialysin
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Lytic Activity and Structural Differences of Amphipathic Peptides Derived from Trialysin

机译：Trialysin衍生的两亲性肽的裂解活性和结构差异

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Trialysin is a pore-forming protein found in the saliva of Triatoma infestans (Hemiptera,Reduviidae),the insect vector of Chagas' disease.The protein is active against a broad range of cell types from bacteria to eukaryotic cells.Recognizing that the N-terminus of trialysin harbors the lytic motif [Amino,R.,Martins,R.M.,Procopio,J.,Hirata,I.Y.,Juliano,M.A.,and Schenkman,S.(2002) J.Biol.Chem.277,6207-6213],we designed a set of peptides scanning this region to investigate the structural basis of its biological function.Peptides encompassing residues 1-32 (P6),1-27 (P7),and 6-32 (P5) efficiently induced lysis of the protozoan parasite Trypanosoma cruzi and Escherichia coli in the 0.4-9.0 mu M range,while much higher concentrations were required to cause hemolysis.Other more internal peptides,including peptide P2 (residues 21-47) and others up to residue 52,were less effective.P6 turned out to be the most active of all.P7 has a significantly higher activity than P5 against E.coli,while P5 has a hemolytic activity comparable to that of P6.CD spectroscopy showed that all tested peptides acquire a comparable helical content in solvent mixtures or in detergent micelles.The solution structure of P2 and P5-P7 was determined in a 30% trifluoroethanol/water mixture by nuclear magnetic resonance.All peptides exhibit a structure characterized by a central helical fold,and except for P2,which does not show a continuous hydrophobic surface,they are amphipathic.The structural models show that P5 and P7 extend their structural similarities with the most active peptide,P6,in either the C-terminus or the N-terminus.Amino acid substitutions in the N-terminus of P6 improved hemolysis but did not change the activity against T.cruzi.These results suggest that while amphipathicity is essential for the lytic activity,the selectivity of the active peptides for specific organisms appears to be associated with the structural features of their N- and C-termini.
机译：Trialysin是在Chagas病的昆虫载体Triatoma infestans（Hemiptera，Reduviidae）的唾液中发现的一种成孔蛋白。该蛋白对从细菌到真核细胞的多种细胞类型均具有活性。三叶草毒素的末端具有裂解基序[Amino，R.，Martins，RM，Procopio，J.，Hirata，IY，Juliano，MA，and Schenkman，S。（2002）J.Biol.Chem.277,6207-6213] ，我们设计了一组扫描该区域的肽以研究其生物学功能的结构。包含残基1-32（P6），1-27（P7）和6-32（P5）的肽可有效诱导原生动物的裂解寄生虫克氏锥虫和大肠杆菌在0.4-9.0μM范围内，而引起溶血则需要更高的浓度。其他更多的内部肽，包括P2肽（21-47位残基）和其他52位残基，效果较差。 P6是最活跃的。P7的抗大肠杆菌活性明显高于P5，而P5具有与P6相当的溶血活性.CD光谱表明，所有测试的肽在溶剂混合物或去污剂胶束中均具有可比的螺旋含量.P2和P5-P7的溶液结构是在30％三氟乙醇/水混合物中测定的所有肽均具有中心螺旋折叠特征，并且除P2以外不显示连续的疏水表面，它们都是两亲性的。结构模型表明P5和P7扩展了它们的结构相似性，并具有最强的活性。 C末端或N末端的肽段P6.P6 N末端的氨基酸取代改善了溶血作用，但并未改变其对T.cruzi的活性。这些结果表明，两亲性对于溶血至关重要活性肽对特定生物的选择性似乎与其N和C末端的结构特征有关。

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