Antimicrobial peptides(AMPs),with their extraordinary properties,such as broad-spectrum activity,rapid action and difficult development of resistance,have become promising molecules as new antibiotics.Despite their va...Antimicrobial peptides(AMPs),with their extraordinary properties,such as broad-spectrum activity,rapid action and difficult development of resistance,have become promising molecules as new antibiotics.Despite their various mechanisms of action,the interaction of AMPs with the bacterial cell membrane is the key step for their mode of action.Moreover,it is generally accepted that the membrane is the primary target of most AMPs,and the interaction between AMPs and eukaryotic cell membranes(causing toxicity to host cells)limits their clinical application.Therefore,researchers are engaged in reforming or de novo designing AMPs as a‘singleedged sword’that contains high antimicrobial activity yet low cytotoxicity against eukaryotic cells.To improve the antimicrobial activity of AMPs,the relationship between the structure and function of AMPs has been rigorously pursued.In this review,we focus on the current knowledge of α-helical cationic antimicrobial peptides,one of the most common types of AMPs in nature.展开更多
Secondary structure of [Val. Ala]sCT- an analog of salmon calcitonin (sCT) not containing an N-terminal disultide bridge. was investigated by circular dichroism (CD) and Fourier-transform intrared spectroscopy (FTIR) ...Secondary structure of [Val. Ala]sCT- an analog of salmon calcitonin (sCT) not containing an N-terminal disultide bridge. was investigated by circular dichroism (CD) and Fourier-transform intrared spectroscopy (FTIR) methods. Both CD and FTIR results show that the main contbrmational structure of [Val Ala']sCT in aqueous solution is random coil structure. while in trifluorethanol (TFE) it displays a strong α-helical structure. The relationship between the biological activity and the conformational structure of [Val, Ala] sCT is als0 discussed.展开更多
基金This work was supported by Natural Science Foundation of China Grant No.30840029Grants for Doctorate Program of New Teacher,Ministry of Education of China,No.20070183062,No.200801831064the Excellent Youth Program of the Jilin Provincial Science&Technology Department,China,Grant No.20070111.
文摘Antimicrobial peptides(AMPs),with their extraordinary properties,such as broad-spectrum activity,rapid action and difficult development of resistance,have become promising molecules as new antibiotics.Despite their various mechanisms of action,the interaction of AMPs with the bacterial cell membrane is the key step for their mode of action.Moreover,it is generally accepted that the membrane is the primary target of most AMPs,and the interaction between AMPs and eukaryotic cell membranes(causing toxicity to host cells)limits their clinical application.Therefore,researchers are engaged in reforming or de novo designing AMPs as a‘singleedged sword’that contains high antimicrobial activity yet low cytotoxicity against eukaryotic cells.To improve the antimicrobial activity of AMPs,the relationship between the structure and function of AMPs has been rigorously pursued.In this review,we focus on the current knowledge of α-helical cationic antimicrobial peptides,one of the most common types of AMPs in nature.
文摘Secondary structure of [Val. Ala]sCT- an analog of salmon calcitonin (sCT) not containing an N-terminal disultide bridge. was investigated by circular dichroism (CD) and Fourier-transform intrared spectroscopy (FTIR) methods. Both CD and FTIR results show that the main contbrmational structure of [Val Ala']sCT in aqueous solution is random coil structure. while in trifluorethanol (TFE) it displays a strong α-helical structure. The relationship between the biological activity and the conformational structure of [Val, Ala] sCT is als0 discussed.
