The resistance of microorganisms to antibiotics is occurring worldwide. An alternative against resistant bacteria has been antimicrobial peptides. Cell penetrating peptides are a family of peptides that are able to cross the biological membrane. In the present study, the peptide desCys11/Lys12/Lys13(p-BthTX-I)2K was coupled to the cell penetrating peptides PFVYLI, HIV-TAT (47-57) and AIP-6 to improve its antimicrobial action. The peptides were synthesized by SPPS. Circular dichroism spectroscopy was used to evaluated structure of conjugates. The biological activity was determined by broth microdilution tests and the minimum inhibitory concentration and the minimum bactericidal concentration were obtained. The hemolytic activity was performed to measure the toxicity against erythrocytes. The results obtained demonstrate that the peptides do not have a defined structure, which is consistent with the structure of desCys11/Lys12/Lys13(p-BthTX-I)2K. Conjugates showed activity against Gram-negative E. coli similar to the wild type peptide. However, the MIC decreased from 128 µM to values between 16 µM and 8 µM in Gram-positive S. aureus. Except to PFVYLI conjugate, hemolytic activity was not found. These results showed that the addition of the fusion peptides to the original peptide, improves the activity of the peptide against Gram-positive bacteria, without decrease its activity in Gram-negative bacteria.
Previous Article in event
Previous Article in session
Next Article in event
Antibacterial Activity of DesCys11/Lys12/Lys13-(p-BthTX-I)2K Sequence Conjugated to Cell-Penetrating Peptides
Published:
27 May 2021
by MDPI
in First Canadian Peptide and Protein Community Virtual Symposium
session Peptide and Protein Applications in Cosmetic, Agricultural and High-tech Products
https://doi.org/10.3390/CPPC2021-10216
(registering DOI)
Abstract:
Keywords: Antimicrobial peptides; cell penetration peptides; p-BthTX-I; bacterial resistance.