Membranolytic antifungal activity of arenicin-1 requires the N-terminal tryptophan and the beta-turn arginine.
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.
Park
Cana
C
School of Life Sciences and Biotechnology, College of Natural Sciences, Kyungpook National University, 1370 Sankyuk-dong, Puk-ku, Daegu, 702-701, Republic of Korea.
Cho
Jaeyong
J
Lee
Juneyoung
J
Lee
Dong Gun
DG
D000935:Antifungal Agents / Q000737:chemistry / Q000494:pharmacology*; D023181:Antimicrobial Cationic Peptides; D001120:Arginine / Q000235:genetics*; D002942:Circular Dichroism; D015801:Helminth Proteins; D008826:Microbial Sensitivity Tests; D016297:Mutagenesis, Site-Directed; D050505:Mutant Proteins / Q000737:chemistry / Q000235:genetics / Q000494:pharmacology; D010455:Peptides / Q000737:chemistry / Q000235:genetics* / Q000494:pharmacology*; D011487:Protein Conformation; D017384:Sequence Deletion; D013050:Spectrometry, Fluorescence; D013329:Structure-Activity Relationship; D014364:Tryptophan / Q000235:genetics*
D000935:Antifungal Agents; D023181:Antimicrobial Cationic Peptides; D015801:Helminth Proteins; D050505:Mutant Proteins; D010455:Peptides; C496888:arenicin-1, Arenicola marina; D014364:Tryptophan; D001120:Arginine