One prime focus in our group is structural analysis of protein fibrillation. We analyse fibrillating proteins during the fibrillation process, in a time-resolved manner. This has enabled us to present the first ever solution structure of a structural fibrillation nucleus (Vestergaard, Groenning et al. 2008), based on data from maturing insulin fibrils. On-going projects include analysis of Parkinson's-related alpha-synuclein, human transthyretin (associated with senile systemic amyloidosis), the Alzheimers related amyloid-beta, glucagon-like peptide 2, and selected model peptides from fibrillation-prone proteins. The vision of our group, is to establish a full structural understanding of protein fibrillation.

analysis of insulin fibrillation

Figure 1: Solution models, derived by SAXS analysis of insulin fibrillation. An idealized trace of the calculated volume fractions of insulin monomers (grey), intermediate oligomer (purple) and mature fibrils (blue) is shown in the background versus time. Superimposed are the surface representations of a monomeric insulin molecule and SAXS derived ab initio models of the oligomer and fibril respectively, shown in the same colours. The insulin monomer is to scale with the oligomer, and a 200 Å length scale is shown next to the insulin oligomer and fibril repeating unit respectively. Note that only one repeating unit of the fibril is modelled from the SAXS data (shown in more intense blue color). The intertwining fibril has been modelled by simple translation of individual repeats. Modified from (Langkilde & Vestergaard (2012)).


























































Group leader

Group Leader

Annette Eva Langkilde
Associate Professor

Phone +45 3533 6202>

Group/project members

Internal researchers

Name Title Phone E-mail
Langkilde, Annette Eva Associate Professor +4535336202 E-mail
Vestergaard, Bente Professor, Emerita +4535336403 E-mail