Investigation of human β-defensins 1, 2 and 3 in human saliva by molecular dynamics

Abstract

Human beta-defensins present in saliva have a broad spectrum of antimicrobial activities that work against infections in oral cavity. To provide a better understanding of these molecules' properties and functions at the molecular level, we have investigated and compared the important structural properties of human beta-defensin-1, -2 and -3 using molecular dynamics simulations. Our results have shown that human beta-defensin-3 has a more flexible structure in water than the other two because of its high hydrophilicity, low beta-sheet content and high repulsive forces between its charged residues. Moreover, we found that the location of the salt bridges is important in protein's stability in water.