Modelling study of dimerization in mammalian defensins

Background: Defensins are antimicrobial peptides of innate immunity functioning by non-specific binding to anionic phospholipids in bacterial membranes. Their cationicity, amphipathicity and ability to oligomerize are considered key factors for their action. Based on structural information on human -defensin 2, we examine homologous defensins from various mammalian species for conserved functional physico-chemical characteristics. Results: Based on homology greater than 40%, structural models of 8 homologs of HBD-2 were constructed. A conserved pattern of electrostatics and dynamics was observed across 6 of the examined defensins; models backed by energetics suggest that the defensins in these 6 organisms are characterized by dimerization-linked enhanced functional potentials. In contrast, dimerization is not energetically favoured in the sheep, goat and mouse defensins, suggesting that they function efficiently as monomers. Conclusion: -defensin 2 from some mammals may work as monome...

• Type: Journal
• Year: 2006
• Where: BMCBI
• Authors: Anita Suresh, Chandra Verma
• Keywords: BMCBI 2006, Defensins, Innate Immunity, Peptides