Libo Yuan, Ke Wang, Yuan Fang, Xiujuan Xu, Yingcun Chen, Dongxin Zhao, Kui Lu
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引用次数: 0
摘要
Cecropin A（1-7）是一种阳离子抗菌肽，含有大量碱性氨基酸。为了了解碱性氨基酸对 Cecropin A (1-7) 的影响，我们设计并合成了在 N 端或 C 端含有更多精氨酸或赖氨酸的类似物 CA2、CA3 和 CA4。利用紫外-可见光谱、荧光光谱和圆二色光谱研究了麦角蛋白 A（1-7）及其类似物与 DNA 的相互作用。多光谱分析显示，碱性氨基酸改善了类似物与 DNA 之间的相互作用。CA4 与 DNA 的相互作用最为明显。荧光光谱显示，CA4 的 Ksv 值为 1.19 × 105 L mol-1，而原肽 cecropin A (1-7) 的 Ksv 值为 3.73 × 104 L mol-1。用 cecropin A (1-7) 及其类似物进行的抗菌实验结果表明，碱性氨基酸增强了类似物的抗菌效果。CA4 对大肠杆菌的抗菌活性是麦角素 A（1-7）的 8 倍。这揭示了碱性氨基酸在肽中的重要性，为后续的抗菌肽研究提供了有用的信息。
Interaction of Cecropin A (1–7) Analogs with DNA Analyzed by Multi-spectroscopic Methods
Cecropin A (1–7) is a cationic antimicrobial peptide which contain lots of basic amino acids. To understand the effect of basic amino acids on cecropin A (1–7), analogues CA2, CA3 and CA4 which have more arginine or lysine at the N-terminal or C-terminal were designed and synthesized. The interaction of cecropin A (1–7) and its analogs with DNA was studied using ultraviolet–visible spectroscopy, fluorescence spectroscopy and circular dichroism spectroscopy. Multispectral analysis showed that basic amino acids improved the interaction between the analogues and DNA. The interaction between CA4 and DNA is most pronounced. Fluorescence spectrum indicated that Ksv value of CA4 is 1.19 × 105 L mol−1 compared to original peptide cecropin A (1–7) of 3.73 × 104 L mol−1. The results of antimicrobial experiments with cecropin A (1–7) and its analogues showed that basic amino acids enhanced the antimicrobial effect of the analogues. The antimicrobial activity of CA4 against E. coli was eightfold higher than that of cecropin A (1–7). The importance of basic amino acid in peptides is revealed and provides useful information for subsequent studies of antimicrobial peptides.
期刊介绍：
The Protein Journal (formerly the Journal of Protein Chemistry) publishes original research work on all aspects of proteins and peptides. These include studies concerned with covalent or three-dimensional structure determination (X-ray, NMR, cryoEM, EPR/ESR, optical methods, etc.), computational aspects of protein structure and function, protein folding and misfolding, assembly, genetics, evolution, proteomics, molecular biology, protein engineering, protein nanotechnology, protein purification and analysis and peptide synthesis, as well as the elucidation and interpretation of the molecular bases of biological activities of proteins and peptides. We accept original research papers, reviews, mini-reviews, hypotheses, opinion papers, and letters to the editor.
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