Related Experiment Video
Updated: Jul 5, 2025

CD Spectroscopy to Study DNA-Protein Interactions
Published on: February 10, 2022
Interaction of Cecropin A (1-7) Analogs with DNA Analyzed by Multi-spectroscopic Methods
Libo Yuan1, Ke Wang2, Yuan Fang3
1College of Chemistry and Chemical Engineering, Henan University of Technology, Zhengzhou, 450001, People's Republic of China. lbyuan@haut.edu.cn.
Abstract:
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.

