ß-defensins are a family of cationic, cysteine-rich antimicrobial peptide (AMP) components of
the innate immune response to infection. They are expressed both inducibly and constitutively
within vertebrates, insects and plants and antimicrobial action is observed against (both gram
positive and gram negative) bacteria and a subset of enveloped viruses. The antimicrobial
phenomenon is thought to result from membrane permeablisation that depends on key,
electrostatic binding events between defensin and pathogen cell surface. This thesis tackles, in
silico, two components of this structure-activity problem: That of rationally predicting ß-defensin structure, and that of elucidating the first (presumed) binding events between ß-defensin and pathogen cell surface. Preliminary results suggest that successful in silico folding
requires a mobile disulphide bond strategy to circumvent kinetic trapping of intermediate states,
and that the mechanism of pathogenic binding involves a complex interplay of hydrogen
bonding, as well as productive electrostatic interactions
