INVESTIGADORES
PEREZ Luis Orlando
congresos y reuniones científicas
Título:
Cationic Hylin Bioactive Peptides from Boana pulchella (Anura: Hylidae): Activity, Structure, and Interaction with Lipid Membranes
Autor/es:
AGUILAR, SILVANA; BRUNETTI, ANDRÉS E.; GARAY, AISEL VALLE; SANTOS, LIEM CANET; PÉREZ, LUIS ORLANDO; MOREIRA, DANIEL; CANCELARICH, NATALIA L.; ALVES BARBOSA EDER; BASSO, NÉSTOR GUILLERMO; DE FREITAS, SONIA MARIA; FAIVOVICH, JULIÁN; BRAND, GUILHERME; CABRERA, GABRIELA M.; LEITE, JOSÉ R.S.A.; MARANI, MARIELA MIRTA
Lugar:
Sitges
Reunión:
Simposio; 36th European and the 2th International Peptide Symposium; 2022
Resumen:
Introduction. Pathogens generate different defense mechanisms in order to tolerate the effects of conventional antibiotics, which causes a global health problem. Amphibians have a great diversity of bioactive peptides in their skin. This makes them an important source of novel peptides that can be used as antibacterials. Objective. Identify and characterize novel peptides from the skin of the tree frog Boana pulchella. Evaluate the secondary structure that these peptides adopt in thepresence of neutral and anionic membrane environments and elucidate the potential mechanism of action of these molecules. Results. Identificación of five novel peptides. Their features favor nonspecific interactions with bacterial membranes that initiate with an electrostatic attraction to the net negative charge of the outer surface of bacteria and proceed through the aggregation of AMPsin the bacterial membrane, affecting its integrity and leading to cell death. Conclusion. The inhibitory action of these peptides, as well as their interaction with lipid vesicles suggests they exert their effect through nonspecific interaction with bacterial membranes. This study highlights the relevance of the membrane environment to induce a stable conformation and enhanced activity of these peptides against bacteria. Analogues were designed and synthesized in a rational way and will be characterized to obtain improved-performance peptides.