File(s) under permanent embargo
Expression and analysis of heparin-binding regions of the amyloid precursor protein of Alzheimer's disease
journal contribution
posted on 2023-05-17, 10:03 authored by Mok, SS, Sberna, G, Heffernan, D, Cappai, R, Galatis, D, Clarris, HJ, Sawyer, WH, Beyreuther, K, Masters, CL, David SmallDavid SmallDeletion mutagenesis studies have suggested that there are two domains within APP which bind heparan sulphate. These domains have been cloned and expressed in the yeast Pichia pastoris. Both recombinant proteins bound to heparin. One domain (APP316–447) was further characterised by binding studies with peptides encompassing this region. Peptides homologous to APP316–346 and APP416–447 were found to bind heparin. Circular dichroism studies show that APP416–447 shifted towards an α-helical conformation in the presence of heparin. This study suggests that heparin-binding domains may lie within regions high in α-helical structure.
History
Publication title
F E B S Letters: (Federation of European Biochemical Societies)Volume
415Pagination
303-307ISSN
0014-5793Department/School
Menzies Institute for Medical ResearchPublisher
Elsevier Science BvPlace of publication
Po Box 211, Amsterdam, Netherlands, 1000 AeRights statement
The definitive version is available at http://www.sciencedirect.comRepository Status
- Restricted