Peptides DLL37-1 and LL37-1, an alternative to inhibit biofilm formation in clinical isolates of Staphylococcus aureus and Staphylococcus epidermidis.

Staphylococcus aureus and Staphylococcus epidermidis have microbial surface components recognizing adhesive matrix molecules (MSCRAMM) adhesion proteins that enhance their biofilm formation ability, as well as virulence factors that influence morbidity and mortality in hospital settings. In this work, four peptides analogous of the peptide LL-37 that were evaluated to inhibit biofilm formation and its action potential on the expression of MSCRAMM proteins in clinical isolates through different tests, such as crystal violet, PCR and qPCR. In total, 96.

Synergistic bactericide and antibiotic effects of dimeric, tetrameric, or palindromic peptides containing the RWQWR motif against Gram-positive and Gram-negative strains.

Dimeric and tetrameric peptides derived from LfcinB (20-25): RRWQWR, LfcinB (20-30): RRWQWRMKKLG, LfcinB (17-31): FKARRWQWRMKKLGA, or the palindromic sequence LfcinB (21-25): RWQWRWQWR were obtained by means of the SPPS-Fmoc/Bu methodology. The antibacterial activity of these molecules was evaluated against (ATCC 25922 and ATCC 11775), (ATCC 25923), (ATCC 29212), and (ATCC 27853). The dimer LfcinB (20-25): (RRWQWR)K-Ahx, the tetramer LfcinB (20-25): (RRWQWR)K-Ahx-C, and the palindromic sequence LfcinB (21-25) exhibited the highest antibacterial activity against the tested bacterial strains.