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Título : Picturins and Pictuseptins, two novel antimicrobial peptide families from the skin secretions of the Chachi treefrog, Boana picturata
Autor : Morán Marcillo, Giovanna
Sánchez Hinojosa, Verónica
Espinosa de Los Monteros Silva, Nina
Blasco Zúñiga, Ailín
Rivera, Miryan
Naranjo, Renato E
De Almeida, José R.
Wang, Lei
Chen, Tianbao
Zhou, Mei
Shaw, Chris
Proaño Bolaños, Carolina
Palabras clave : Antibacterial;
Synthetic peptides
Frog skin secretion
Fecha de publicación : 2022
Citación : Morán-Marcillo G, Sánchez Hinojosa V, de Los Monteros-Silva NE, Blasco-Zúñiga A, Rivera M, Naranjo RE, Almeida JR, Wang L, Zhou M, Chen T, Shaw C, Proaño-Bolaños C. Picturins and Pictuseptins, two novel antimicrobial peptide families from the skin secretions of the Chachi treefrog, Boana picturata. J Proteomics. 2022 Jul 30;264:104633. doi: 10.1016/j.jprot.2022.104633. Epub 2022 May 29. PMID: 35640793.
Resumen : The Imbabura treefrog (Boana picturata) is an underexplored source of bioactive peptides. The combination of molecular cloning and mass spectrometry allowed us to identify three new peptide families, named "Picturins" (PTR), "Pictuseptins" (PTS), and "Boanins" (BNS). PTR is composed of three 25-mer peptides, characterized by the N-terminal sequence: GVFKDALKQ and the C-terminal sequence: AANALKPK. The sequences of PTR-1, -2 and - 3 are highly conserved only showing two divergent sites: (L/F) in position 10 and (K/Q) in position 17. PTS gathers six peptides. PTS -1, -2 and - 4 have 22 amino acid residues in length, while PTS -3, -5 and - 6 are composed of 26 residues. Whereas BNS are four 28-37 mer peptides, showing two conserved regions: the N-terminal sequence FLGAL and the C-terminal sequence KALNP. PTR-1 to 3 and PTS -1 to -3 were chemically synthetized and their antimicrobial and haemolytic activity was assessed. PTR displayed moderate activity against Escherichia coli (MIC 24.80 to 48.95 μM), while PTS showed a broad antimicrobial and antifungal effect. PTS-1 was the most active peptide against E. coli (6.8 μM) followed by PTS-3 (11.7 μM) and PTS-2 (14.24 μM). These peptides also showed low haemolytic activity, pointing to a favorable selectivity. Overall, new unique non-hemolytic and cationic peptide sequences were characterized that could be valuable for the next-generation of anti-infective drugs. Future functional studies should explore the pharmacological potential of Boanins to include them as antimicrobial scaffolds. BIOLOGICAL SIGNIFICANCE: Nature-inspired solutions have shown their importance mainly for the development of the pharmaceutical industry. Frog skin peptides are excellent examples of the biomedical potential of naturally evolved molecules for specific targets, including multi-resistant bacteria. The characterization of new chemical entities from poorly studied skin secretions of Ecuadorian biodiversity, such as B. picturata, represents an unprecedented opportunity to identify candidates to tackle global concerns, for instance, antibiotic resistance.
URI : http://repositorio.ikiam.edu.ec/jspui/handle/RD_IKIAM/577
ISSN : doi: 10.1016/j.jprot.2022.104633
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