Antimicrobial Cyanopeptide Action on Bacterial Cells Observed with Atomic Force Microscopy
Maria Estela Silva-Stenico,
Adriana Sturion Lorenzi,
Caroline Souza Pamplona Silva,
Marli Fatima Fiore.
Cyanobacteria produce oligopeptides that are predominantly synthesized by the non-ribosomal pathway. Among these are the
aeruginosin and cyanopeptolin protease inhibitors, which act against enzymes known to cause several human health problems. Atomic
force microscopy (AFM) was used to study the effect of cyanopeptides produced by Microcystis aeruginosa NPCD-1 on pathogenic bacterial
cell surfaces. The selected strain was characterized based on the 16S rRNA gene sequence and the intergenic spacer region of the
phycocyanin operon. PCR amplification was employed to investigate the presence of genes encoding for aeruginosin and cyanopeptolin.
Purified extract from M. aeruginosa NPCD-1 cells was screened for bioactive compounds. The effect of purified extract containing protease
inhibitors produced by the NPCD-1 strain on bacterial cells was observed using AFM. Aeruginosin and cyanopeptolin genes were
confirmed by both PCR amplification and gene sequencing. Mass spectrometry analysis confirmed the production of aeruginosin. The interaction
of Bacillus cereus, Escherichia coli and Staphylococcus aureus with cyanopeptides was characterized by examining the loss of
surface stiffness and the formation of micelles, most likely originating from the membrane disruption. The AFM results demonstrate the
ability of cyanobacterial extract to alter the cellular membrane of bacterial pathogens.
Keywords: Aeruginosin, atomic force microscopy, cyanobacteria, cyanopeptolin, mass spectrometry, protease inhibitor
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