ALL-D-MAGAININ - CHIRALITY, ANTIMICROBIAL ACTIVITY AND PROTEOLYTIC RESISTANCE
ALL-D-MAGAININ - CHIRALITY, ANTIMICROBIAL ACTIVITY AND PROTEOLYTIC RESISTANCE
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DOI：
10.1016/0014-5793(90)81351-n
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发表时间：
1990-11-12
期刊：
影响因子：
3.5
通讯作者：
FRIDKIN, M
中科院分区：
文献类型：
--
作者：
BESSALLE, R;KAPITKOVSKY, A;FRIDKIN, M
合成了All-D-magainin-2，实验证实了表面活性肽的生物学功能主要源于其独特的两亲性α -螺旋结构。事实上，肽表现出抗菌效力几乎相同的全l-对映体。对蛋白水解和非溶血性全d -镁蛋白具有高度抗性，可能具有相当大的治疗意义。
All-D-magainin-2 was synthesized to corroborate experimentally the notion that the biological function of a surface-active peptide stems primarily from its unique amphiphilic α -helical structure. Indeed, the peptide exhibited antibacterial potency nearly identical to that of the all-L-enantiomer. Being highly resistant to proteolysis and non-hemolytic all-D-magainin might have considerable therapeutic importance.