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A designed catioinic, amphiphilic peptide was previously shown to bind porphyrin molecules and promote the formation of excitonically coupled J-aggregate structures (Caputo et. al. 2009). Due to the catioinic and… Click to show full abstract
A designed catioinic, amphiphilic peptide was previously shown to bind porphyrin molecules and promote the formation of excitonically coupled J-aggregate structures (Caputo et. al. 2009). Due to the catioinic and amphiphilic nature, this peptide was investigated for antimicrobial activity. We synthesized 3 variants of the peptide which differed only in the position of a single Trp residue, used as a reporter of membrane binding interactions. All three variants showed similar levels of antimicrobial activity against Gram+ and G- strains (low micromolar efficacy).
Journal Title: Biophysical Journal
Year Published: 2017
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