Structure and antimicrobial activity of peptide CGA- N46 and its derived peptides
LI Ruifang;SUN Yanan;CHENG Yanbo;LU Zhifang;College of Biological Engineering,Henan University of Technology;
To study the structure and antimicrobial activity of CGA- N46 and its derived peptides CGA- N16,CGA- N12 and to find high effective antifungal compounds,the bioinformatics software was used to predict the spatial structure of CGA- N46 and its derived peptides CGA- N16 and CGA- N12,circular dichroism( CD)was used to study the secondary structures under different environmental conditions,and the antimicrobial activity was measured with MTT assay. The results showed that CGA- N46,CGA- N16 and CGA- N12 were predicted to be positively charged,hydrophilic,alpha helical peptides; the secondary structure of the peptides in aqueous solution and 30 m M SDS solution were alpha helix,but changed in liposome solution,the proportion of alpha helix reduced,and other structures' proportion increased. The MTT experimental results showed that CGA-N46,CGA- N16 and CGA- N12 present strong antifungal activity,but have no inhibitory effect on bacteria growth. With the secondary structure changing,the antimicrobial activity of CGA- N46 and its derived peptides CGA- N16,CGA- N12 changed. These results laid a foundation for the research of its mechanism of action.