Zganec Matjaž, Zerovnik Eva
Department of Biochemistry and Molecular and Structural Biology, Jožef Stefan Institute, Jamova 39, Ljubljana, Slovenia; Faculty of Mathematics and Physics, University of Ljubljana, Jadranska 19, Ljubljana, Slovenia.
Department of Biochemistry and Molecular and Structural Biology, Jožef Stefan Institute, Jamova 39, Ljubljana, Slovenia; CipKeBip - Center of Excellence for integrated approaches in chemistry and biology of proteins, Jamova 39, 1000 Ljubljana, Slovenia.
Biochim Biophys Acta. 2014 Sep;1840(9):2944-52. doi: 10.1016/j.bbagen.2014.05.019. Epub 2014 Jun 5.
Prefibrillar oligomeric states and amyloid fibrils of amyloid-forming proteins qualify as nanoparticles. We aim to predict what biophysical and biochemical properties they could share in common with better researched peptide nanotubes. We first describe what is known of amyloid fibrils and prefibrillar aggregates (oligomers and protofibrils): their structure, mechanisms of formation and putative mechanism of cytotoxicity. In distinction from other neuronal fibrillar constituents, amyloid fibrils are believed to cause pathology, however, some can also be functional. Second, we give a review of known biophysical properties of peptide nanotubes. Finally, we compare properties of these two macromolecular states side by side and discuss which measurements that have already been done with peptide nanotubes could be done with amyloid fibrils as well.
