I recommend this paper
The study describes an elegant tool for what has been a frustrating problem. Of particular interest to us, this study shows that Aβ dimers have striking structural similarities to the dimeric forms of the antimicrobial peptides human NP2, horseshoe crab tachystatin B, and mouse α-defensin. We recently reported on the antimicrobial activity of Aβ, and our newest data suggest dimerization is a key event in turning relatively inactive Aβ monomers into forms that can attack bacteria.
This is not a phenomenon restricted to Aβ. It has been known for some time that oligomerization has an important role in the action and targeting of a number of antimicrobial proteins (AMPs), including the archetypal antimicrobial peptide LL-37 which can form oligomers, fibrils, and birefringent amyloid (albeit, LL-37 amyloid has only been observed in vitro to date). Oligomerization is also a key mechanism for antimicrobial protein-mediated agglutination and inactivation of viral particles.
Despite this central role in AMP mechanisms, relatively few studies have characterized the oligomerization...