Enhanced membrane pore formation by Multimeric/Oligomeric antimicrobial peptides
Enhanced membrane pore formation by Multimeric/Oligomeric antimicrobial peptides
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DOI：
10.1021/bi7015553
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发表时间：
2007-11-20
期刊：
影响因子：
2.9
通讯作者：
Pieters, Roland J.
中科院分区：
文献类型：
--
作者：
Arnusch, Christopher J.;Branderhorst, Hilbert;Pieters, Roland J.
通过铜（I）介导的1-3偶极环加成反应（“点击”化学），使成孔抗菌肽爪蟾抗菌肽2成为二价、四价和八价。在体外测试这一系列造孔化合物在大单层囊泡（LUV）中形成孔的能力。在由DOPC组成的LUV中，特别观察到四价和八价爪蟾抗菌肽化合物的成孔能力大幅增加，并且八价爪蟾抗菌肽化合物显示出DOPC/DOPG LUV的显著增加。这些化合物在低纳摩尔范围内观察到活性。
The pore-forming antibacterial peptide magainin 2 was made divalent, tetravalent, and octavalent via a copper(I)-mediated 1-3 dipolar cycloaddition reaction ("click" chemistry). This series of poreforming compounds was tested in vitro for their ability to form pores in large unilamillar vesicles (LUVs). A large increase in the pore-forming capability, was especially observed with the tetravalent and octavalent magainin compounds in the LUVs consisting of DOPC, and the octavalent magainin compound showed a marked increase with the DOPC/DOPG LUVs. Activity was observed in the low nanomolar range for these compounds.