4.4 Article

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

Journal

PEPTIDES
Volume 37, Issue 2, Pages 294-300

Publisher

ELSEVIER SCIENCE INC
DOI: 10.1016/j.peptides.2012.07.017

Keywords

Pg-AMP1; Antimicrobial peptides; Heterologous expression; Psidium guajava

Funding

  1. CNPq
  2. FAPEMIG
  3. CAPES
  4. UCB
  5. UFJF
  6. FAPDF

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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. (C) 2012 Elsevier Inc. All rights reserved.

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