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Peptides. 2012 Oct;37(2):294-300. doi: 10.1016/j.peptides.2012.07.017. Epub 2012 Jul 27.

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

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  • 1Departamento de Biologia, Programa de Pós-Graduação em Genética e Biotecnologia, Universidade Federal de Juiz de Fora, Campus Universitário, 36036-900, Martelos, Juiz de Fora-MG, Brazil.


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.

Copyright © 2012 Elsevier Inc. All rights reserved.

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