Abstract
In a previous study, we found an antifungal effect on human pathogenic fungi by the cell-penetrating peptide Tat (47-58) derived from HIV-1. Tat (47-58) immediately entered into the fungal nucleus and affected some physiological changes on the intracellular condition. In this study, Tat (47-58) showed a broad spectrum of antibacterial activity against pathogenic bacteria including bacterial clinical isolates. To improve resistance against proteases for use in vivo, we synthesized an analog of Tat (47-58) by substituting the L-amino acid for the D-amino acid. The D-enantiomer of Tat (47-58) also exhibited a broad spectrum of antibacterial activity at almost the same level of L-Tat (47-58) concentration. Unlike L-Tat (47-58), D-Tat (47-58) showed a significant proteolytic resistance against all proteases tested and antimicrobial activities in the presence of trypsin. Moreover, D-Tat (47-58) inhibited MRSA infection in human HeLa cells whereas L-Tat (47-58) partially allowed MRSA infection, and the results were due to the proteolytic resistance of D-Tat (47-58).
| Original language | English (US) |
|---|---|
| Pages (from-to) | 990-996 |
| Number of pages | 7 |
| Journal | Journal of Microbiology and Biotechnology |
| Volume | 18 |
| Issue number | 5 |
| State | Published - May 28 2008 |
| Externally published | Yes |
Keywords
- Antibacterial activity
- Cell-penetrating peptide
- MRSA infection
- Proteolytic resistance
- Tat (47-58)
ASJC Scopus subject areas
- Biotechnology
- Applied Microbiology and Biotechnology