Membranolytic antifungal activity of arenicin-1 requires the N-terminal tryptophan and the beta-turn arginine

作者：Park Cana; Cho Jaeyong; Lee Juneyoung; Lee Dong Gun^*

来源：Biotechnology Letters, 2011, 33(1): 185-189.

DOI：10.1007/s10529-010-0402-x

• Analogues
• Antimicrobial peptide
• Arenicin-1
• Arenicola marina
• Liposome

To determine the structural requirements of arenicin-1 in exerting antifungal activity, a truncated peptide with an N-terminal deletion and a peptide with an Ala substitution for an Arg in the beta-turn region were characterised by comparison to arenicin-1. The antifungal activities of the analogues were 25-50% lower than arenicin-1. Trp fluorescence and circular dichroism spectroscopy showed that Trp in the N-terminus contributed to peptide penetration and Arg in the beta-turn to conformational transition. These results suggest that Trp in the N-terminus and Arg in the beta-turn play a pivotal role in the membrane-directed antifungal activity of arenicin-1.

• 出版日期2011-1