What keeps amyloid fibres together?

In their paper based on analysing the structures of disease-relevant ex vivo amyloid fibres, van der Kant et al. describe the key stabilizing interactions within the fibres.

As it turns out, only a minority of the amino acid residues provide the stability of the amyloid core structure. The rest is up for grabs and can form several, energetically similar conformations, providing an explanation how structural polymorphs arise in the various diseases linked to amyloid fibres formed by the same protein.

Lukasz A. Joachimiak wrote a Preview piece titled “The interactions that shape amyloid fibrils in disease” that highlights the publication.

We are also very proud that Structure agreed to use the spectacular cover image Nikos Louros designed for the 4 August 2022 issue of the magazine.

You can read the paper by van der Kant et al. that belongs to the cover image here.