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Oh, J.E., Hong, S.Y. and Lee, K.H. (1999) Structure- activity relationship study: Short antimicrobial peptides. Journal Peptide Ressearch, 53, 41-46. doi:10.1111/j.1399-3011.1999.tb01615.x

has been cited by the following article:

• TITLE: Degradation of naturally occurring and engineered antimicrobial peptides by proteases

  AUTHORS: Bernard J. Moncla, Kara Pryke, Lisa Cencia Rohan, Phillip W. Graebing

  KEYWORDS: Microbicides; HIV; Anti-HIV; Antimicrobial Peptides; Proteases

  JOURNAL NAME: Advances in Bioscience and Biotechnology, Vol.2 No.6, December 5, 2011

  ABSTRACT: 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.