Antonie van Leeuwenhoek

, Volume 111, Issue 10, pp 1871–1882 | Cite as

In silico design of polycationic antimicrobial peptides active against Pseudomonas aeruginosa and Staphylococcus aureus

  • Oscar Hincapié
  • Paula Giraldo
  • Sergio Orduz
Original Paper


Antimicrobial peptides (AMPs) have the potential to become valuable antimicrobial drugs in the coming years, since they offer wide spectrum of action, rapid bactericidal activity, and low probability for resistance development in comparison with traditional antibiotics. The search and improvement of methodologies for discovering new AMPs to treat resistant bacteria such as Staphylococcus aureus, Klebsiella pneumoniae, Acinetobacter baumannii and Pseudomonas aeruginosa are needed for further development of antimicrobial products. In this work, the software Peptide ID 1.0® was used to find new antimicrobial peptide candidates encrypted in proteins, considering the physicochemical parameters characteristics of AMPs such as positive net charge, hydrophobicity, and sequence length, among others. From the selected protein fragments, new AMPs were designed after conservative and semi-conservative modifications and amidation of the C-terminal region. In vitro studies of the antimicrobial activity of the newly designed peptides showed that two peptides, P3-B and P3-C, were active against P. aeruginosa Escherichia coli and A. baumannii with low minimum inhibitory concentrations. Peptide P3-C was also active against K. pneumoniae and S. aureus. Furthermore, bactericidal activity and information on the possible mechanisms of action are described according to the scanning electron microscopy studies.


Cationic antimicrobial peptides Bioinformatics Peptide design Pseudomonas aeruginosa Staphylococcus aureus 



This research has been funded by projects 9727 and 35058 from Universidad Nacional de Colombia, sede Medellin.

Conflict of interest

The authors declare that they have no conflict of interest.


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Copyright information

© Springer International Publishing AG, part of Springer Nature 2018

Authors and Affiliations

  1. 1.Grupo de Investigación de Biología Funcional, Escuela de Biociencias - Facultad de CienciasUniversidad Nacional de ColombiaMedellínColombia

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