摘要
Secondary structure prediction studies on CAP18, a lipopolysaccharide binding protein from rabbit granulocytes, identified a highly cationic, 21-residue sequence with the tendency to adopt an amphipathic -helical conformation, as observed in many antimicrobial peptides. The corresponding peptide was chemically synthesized and shown to exert a potent bacterieidal activity against both Gram-negative and Gram-positive bacteria, and a rapid permeabilization of the inner membrane of Escherichia coli. Five analogues were synthesized to elucidate structure/activity relationships. It was found that helix disruption virtually eliminates antibacterial activity, while the degree of amphipathicity and the presence of an aromatic residue greatly affect the kinetics of bacterial inner membrane permeabilization. .overlined { text-decoration: overline; } .struck { text-decoration:line-through; } .underlined { text-decoration:underline; } .doubleUnderlined { text-decoration:underline;border-bottom:1px solid #000; } Enhanced Article (HTML) Get PDF (700K)Get PDF (700K) More content like thisFind more content: like this articleFind more content written by: Alessandro Tossi Marco Scocchi Barbara Skerlavaj Renato Gennaro All Authors
摘要译文
来自兔粒细胞的脂多糖结合蛋白CAP18的二级结构预测研究鉴定出高度阳离子，21-残基序列具有采用两亲性 - 螺旋构象的倾向，如在许多抗菌肽中所观察到的化学合成相应的肽，显示出对革兰氏阴性菌和革兰氏阳性菌均具有强效的杀菌活性，并合成了大肠杆菌内膜的快速透化.Five类似物，以阐明结构/活性关系发现螺旋破裂实际上消除了抗菌活性，而两亲性的程度和芳香残留物的存在极大地影响细菌内膜透化的动力学。 敲击{text-decoration：line-through; }竨nderlined {text-decoration：underline; }竏oubleUnderlined {text-decoration：underline; border-bottom：1px solid＃000;ML）获取PDF（700K）获取PDF（700K）更多内容喜欢此更多内容：like this article找到更多内容：Alessandro Tossi Marco Scocchi Barbara Skerlavaj Renato Gennaro所有作者
Alessandro Tossi[1]; Marco Scocchi[1]; Barbara Skerlavaj[2] and Renato Gennaro[2];. Identification and characterization of a primary antibacterial domain in CAP18, a lipopolysaccharide binding protein from rabbit leukocytes[J]. FEBS Letters, 1994,339(1-2): 108–112