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Abstract
Antimicrobial peptides (AMPs) are promising antibiotics as they possess strong antimicrobial activity and very broad spectra of activity. However, administration of an antibiotic with a very broad spectrum of activity disrupts normal microflora and increases the risks of other fatal infections. To solve the problem, we designed a novel AMP that is activated by virulent proteases of pathogenic organisms. We constructed a peptide composed of 3 domains, namely, an AMP (lactoferricin) as the active center, a protective peptide (magainin intervening sequence) that suppresses antimicrobial activity, and a specific linker that joins these 2 components and is efficiently cleaved by virulent proteases. We utilized Candida albicans as a model organism that produces secreted aspartic proteases (Saps) as a virulence attribute. We screened for a peptide sequence efficiently cleaved by Sap isozymes, and identified a GFIKAFPK peptide as the most favorable substrate. Subsequently, we chemically synthesized a peptide containing the GFIKAFPK sequence. The designed peptide possessed no antimicrobial activity until it was activated by Sap isozymes. Furthermore, it demonstrated selective antimicrobial activity against C. albicans, but not against Saccharomyces cerevisiae. A designed peptide like the one described in this study may protect normal microflora, resulting in enhanced safety as a therapeutic.
© 2012 John Wiley & Sons A/S
| Authors: | Wataru Aoki, Nao Kitahara, Natsuko Miura, Hironobu Morisaka, Kouichi Kuroda, Mitsuyoshi Ueda | |
| Journal: | Chemical Biology & Drug Design | |
| Year: | 2012 | |
| Pages: | no | |
| DOI: | 10.1111/cbdd.12012 | |
| Publication date: | 02-08-2012 |
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