Buforin II bacteria agglutination activity as part of its antimicrobial action mechanism

Carolina Munoz-Camargo, Vivian Salazar Montoya, Laura Andrea Barrero-Guevara, Helena Groot, Ester Boix

Research output: Contribution to journalArticleResearchpeer-review

2 Citations (Scopus)


Antimicrobial peptides (AMPs) have been found in many multicellular organisms and are considered part of their innate immune system. Several AMP action mechanisms have been described, but recent studies have proposed that a single peptide can use multiple of them. Here we confirm the Buforin II action mechanism already reported and evaluate its capacity to induce bacterial agglutination as part of its action mechanism repertoire. With this purpose, we evaluated and confirmed Buforin II antibacterial activity against Escherichia coli, confirmed its action mechanism in the bacteria and in a membrane model using large unilamellar vesicles (LUVs) and further assessed the peptide agglutination capacity in these two models. Our results show, that Buforin II antibacterial activity against E. coli is accomplished without membrane permeabilization or polarization as reported in previous studies. Furthermore, we report for the first time that Buforin II induces bacteria and LUV agglutination. Hence, here we confirm Buforin II antibacterial action mechanism and describe the bacteria agglutination activity of the peptide.


  • Antimicrobial Peptides
  • Escherichia coli
  • Histone-derived Peptides
  • Host Defense Peptides


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