Send to:

Choose Destination
See comment in PubMed Commons below
Front Microbiol. 2013 Dec 17;4:389. doi: 10.3389/fmicb.2013.00389.

LPS inmobilization on porous and non-porous supports as an approach for the isolation of anti-LPS host-defense peptides.

Author information

  • 1Center for Protein Studies, Faculty of Biology, University of Havana Havana, Cuba.
  • 2Center for Genetic Engineering and Biotechnology Havana, Cuba.
  • 3Centro de Análises Proteômicas e Bioquímicas, Programa de Pós-Graduação em Ciências Genômicas e Biotecnologia, Universidade Católica de Brasília Brasília, Brazil.


Lipopolysaccharides (LPSs) are the major molecular component of the outer membrane of Gram-negative bacteria. This molecule is recognized as a sign of bacterial infection, responsible for the development of local inflammatory response and, in extreme cases, septic shock. Unfortunately, despite substantial advances in the pathophysiology of sepsis, there is no efficacious therapy against this syndrome yet. As a consequence, septic shock syndrome continues to increase, reaching mortality rates over 50% in some cases. Even though many preclinical studies and clinical trials have been conducted, there is no Food and Drug Administration-approved drug yet that interacts directly against LPS. Cationic host-defense peptides (HDPs) could be an alternative solution since they possess both antimicrobial and antiseptic properties. HDPs are small, positively charged peptides which are evolutionarily conserved components of the innate immune response. In fact, binding to diverse chemotypes of LPS and inhibition of LPS-induced pro-inflammatory cytokines from macrophages have been demonstrated for different HDPs. Curiously, none of them have been isolated by their affinity to LPS. A diversity of supports could be useful for such biological interaction and suitable for isolating HDPs that recognize LPS. This approach could expand the rational search for anti-LPS HDPs.


LPS; LPS immobilization; affinity chromatography; antiendotoxic; antimicrobial peptides

Free PMC Article

Publication Types

Publication Types

PubMed Commons home

PubMed Commons

How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Frontiers Media SA Icon for PubMed Central
    Loading ...
    Write to the Help Desk