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Antimicrobial activity of recombinant Pg-AMP1, a glycine-rich peptide from guava seeds

2012; Elsevier BV; Volume: 37; Issue: 2 Linguagem: Inglês

10.1016/j.peptides.2012.07.017

1873-5169

Letícia Stephan Tavares, João Vitor Paes Rettore, Renata Mendes de Freitas, William F. Porto, Ana Paula do Nascimento Duque, Júnya de Lacorte Singulani, Osmar N. Silva, Michelle de Lima Detoni, Eveline Gomes Vasconcelos, Simoni Campos Dias, Octávio Luiz Franco, Marcelo de Oliveira Santos,

Protein Hydrolysis and Bioactive Peptides

Antimicrobial peptides (AMPs) are compounds that act in a wide range of physiological defensive mechanisms developed to counteract bacteria, fungi, parasites and viruses. These molecules have become increasingly important as a consequence of remarkable microorganism resistance to common antibiotics. This report shows Escherichia coli expressing the recombinant antimicrobial peptide Pg-AMP1 previously isolated from Psidium guajava seeds. The deduced Pg-AMP1 open reading frame consists in a 168 bp long plus methionine also containing a His6 tag, encoding a predicted 62 amino acid residue peptide with related molecular mass calculated to be 6.98 kDa as a monomer and 13.96 kDa at the dimer form. The recombinant Pg-AMP1 peptide showed inhibitory activity against multiple Gram-negative (E. coli, Klebsiella pneumonia and Pseudomonas aeruginosa) and Gram-positive (Staphylococcus aureus and Staphylococcus epidermides) bacteria. Moreover, theoretical structure analyses were performed in order to understand the functional differences between natural and recombinant Pg-AMP1 forms. Data here reported suggest that Pg-AMP1 is a promising peptide to be used as a biotechnological tool for control of human infectious diseases.