Degradation of naturally occurring and engineered antimicrobial peptides by proteases  

作　　者：Bernard J. Moncla Kara Pryke Lisa Cencia Rohan Phillip W. Graebing 

机构地区：[1]不详

出　　处：《Advances in Bioscience and Biotechnology》2011年第6期404-408,共5页生命科学与技术进展（英文）

摘　　要：We hypothesized that current antimicrobial peptides should be susceptible to proteolytic digestion. The antimicrobial peptides: Griffithinsin, RC-101, LL-37, LSA-5, PSC-RANTES and DJ007 were degraded by commercially available proteases. Two different species of anaerobic vaginal flora, Prevotella bivia and Porphyromonas asaccharolytica also degraded the materials. Griffithsin was resistant to digestion by 8 of the 9 proteases and the bacteria while LL-37 was the most sensitive to protease digestion. These data suggests most of the molecules may not survive for very long in the proteolytic rich environments in which they are intended to function.We hypothesized that current antimicrobial peptides should be susceptible to proteolytic digestion. The antimicrobial peptides: Griffithinsin, RC-101, LL-37, LSA-5, PSC-RANTES and DJ007 were degraded by commercially available proteases. Two different species of anaerobic vaginal flora, Prevotella bivia and Porphyromonas asaccharolytica also degraded the materials. Griffithsin was resistant to digestion by 8 of the 9 proteases and the bacteria while LL-37 was the most sensitive to protease digestion. These data suggests most of the molecules may not survive for very long in the proteolytic rich environments in which they are intended to function.

关 键 词：MICROBICIDES HIV ANTI-HIV ANTIMICROBIAL PEPTIDES Proteases 

分 类 号：R73[医药卫生—肿瘤]