RESEARCH ARTICLE u T

ha such class is antimicrobial peptides (AMPs), also known However, one drawback of most natural AMPs as thera-Gottschalk et al. BMC Microbiology 2013, 13:192 http://www.biomedcentral.com/1471-2180/13/192amino peptides, but the side chain is shifted to amideSciences, University of Copenhagen, DK-1870 Frederiksberg, DenmarkFull list of author information is available at the end of the articleas host defence peptides, that are found in all multicellu-lar organisms and form an important part of the innate immune system [1]. They exhibit antimicrobial activity against a wide range of pathogenic microorganisms, have immune-modulatory effects and enhance the host de-fence against pathogenic bacteria [2-4]. AMPs are usu-ally small cationic and amphiphatic peptides comprised of less than 40 amino acids with immense diversity in peutics is their susceptibility to proteolytic degradation [6]. To overcome this problem an approach known as peptidomimetics has emerged in recent years by which compounds are produced that mimic a peptide structure and/or function but carries a modified backbone and/or non-natural amino acids. The peptide-mimetic com-pounds have been designed based on essential biophysical characteristics of AMPs: charge, hydrophobicity, and amphiphatic organization [7-9]. Oligomeric N-substituted glycines, also known as peptoids, belong to the simpler AMP-mimetic designs. They are structurally similar to α-* Correspondence