All-D-cecropin B:: Synthesis, conformation, lipopolysaccharide binding, and antibacterial activity

被引：39

作者：

Bland, JM ^{[1
]}

De Lucca, AJ ^{[1
]}

Jacks, TJ ^{[1
]}

Vigo, CB ^{[1
]}

机构：

[1] ARS, USDA, So Reg Res Ctr, New Orleans, LA 70179 USA

来源：

MOLECULAR AND CELLULAR BIOCHEMISTRY | 2001年 / 218卷 / 1-2期

关键词：

all-D-cecropin; solid phase peptide synthesis; circular dichroism conformation; lipopolysaccharide binding; antibacterial activity;

D O I：

10.1023/A:1007293816634

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Cecropin B (LCB) is a natural peptide with antibacterial and antifungal properties. The enantiomer of LCB, containing all-D amino acids (DCB), was synthesized to examine its antibacterial and binding properties. The conformation of DCB was compared to its enantiomer by circular dichroism. Both the L- and D-peptides showed an identical induction of alpha -helical secondary structure. However, binding studies between Lipopolysaccharide (LPS) and DCB or LCB were studied with a dimethylmethylene blue spectrophotometric assay, showing the two enantiomeric peptides differed in their interaction with LPS. Antibacterial activity of DCB was determined against three Gram-negative bacteria, Pantoea agglomerans (ATCC 27996), Escherichia coli (ATCC 8739), and Pseudomonas aeruginosa (ATCC 17648), giving comparable results to LCB.

引用

页码：105 / 111

页数：7

共 27 条

[1] EVALUATION OF SECONDARY STRUCTURE OF PROTEINS FROM UV CIRCULAR-DICHROISM SPECTRA USING AN UNSUPERVISED LEARNING NEURAL-NETWORK [J].