Benincasa Monica, Scocchi Marco, Podda Elena, Skerlavaj Barbara, Dolzani Lucilla, Gennaro Renato
Department of Biochemistry, Biophysics and Macromolecular Chemistry, University of Trieste, Via Giorgieri, 1, I-34127 Trieste, Italy.
Peptides. 2004 Dec;25(12):2055-61. doi: 10.1016/j.peptides.2004.08.004.
Ten peptides from 13 to 35 residues in length and covering the whole sequence of the Pro-rich peptide Bac7 were synthesized to identify the domain responsible for its antimicrobial activity. At least 16 residues of the highly cationic N-terminal sequence were required to maintain the activity against Gram-negative bacteria. The fragments Bac7(1-35) and, to a lesser extent, Bac7(1-16) proved active against a panel of antibiotic-resistant clinical isolates of Gram-negative bacteria, with the notable exception of Burkholderia cepacia. In addition, when tested against fungi, the longer fragment was also active against collection strains and clinical isolates of Cryptococcus neoformans, but not towards clinical isolates of Candida albicans.
合成了10种长度为13至35个残基、覆盖富含脯氨酸肽Bac7整个序列的肽,以确定其抗菌活性的负责结构域。高度阳离子化的N端序列至少需要16个残基才能维持对革兰氏阴性菌的活性。片段Bac7(1-35)以及在较小程度上的Bac7(1-16)对一组革兰氏阴性菌的耐抗生素临床分离株具有活性,但洋葱伯克霍尔德菌是明显的例外。此外,在针对真菌进行测试时,较长的片段对新型隐球菌的标准菌株和临床分离株也有活性,但对白色念珠菌的临床分离株无活性。