| Autor: |
Pablo V M, Reis, Daiane, Boff, Rodrigo M, Verly, Marcella N, Melo-Braga, María E, Cortés, Daniel M, Santos, Adriano M de C, Pimenta, Flávio A, Amaral, Jarbas M, Resende, Maria E, de Lima |
| Rok vydání: |
2017 |
| Předmět: |
|
| Zdroj: |
Frontiers in Microbiology |
| ISSN: |
1664-302X |
| Popis: |
The antimicrobial peptide LyeTxI isolated from the venom of the spider Lycosa erythrognatha is a potential model to develop new antibiotics against bacteria and fungi. In this work, we studied a peptide derived from LyeTxI, named LyeTxI-b, and characterized its structural profile and its in vitro and in vivo antimicrobial activities. Compared to LyeTxI, LyeTxI-b has an acetylated N-terminal and a deletion of a His residue, as structural modifications. The secondary structure of LyeTxI-b is a well-defined helical segment, from the second amino acid to the amidated C-terminal, with no clear partition between hydrophobic and hydrophilic faces. Moreover, LyeTxI-b shows a potent antimicrobial activity against Gram-positive and Gram-negative planktonic bacteria, being 10-fold more active than the native peptide against Escherichia coli. LyeTxI-b was also active in an in vivo model of septic arthritis, reducing the number of bacteria load, the migration of immune cells, the level of IL-1β cytokine and CXCL1 chemokine, as well as preventing cartilage damage. Our results show that LyeTxI-b is a potential therapeutic model for the development of new antibiotics against Gram-positive and Gram-negative bacteria. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
|
