Expression and analysis of heparin-binding regions of the amyloid precursor protein of Alzheimer's disease.

Article Details

Citation

Mok SS, Sberna G, Heffernan D, Cappai R, Galatis D, Clarris HJ, Sawyer WH, Beyreuther K, Masters CL, Small DH

Expression and analysis of heparin-binding regions of the amyloid precursor protein of Alzheimer's disease.

FEBS Lett. 1997 Oct 6;415(3):303-7.

PubMed ID
9357988 [ View in PubMed
]
Abstract

Deletion 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 alpha-helical conformation in the presence of heparin. This study suggests that heparin-binding domains may lie within regions high in alpha-helical structure.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Amyloid beta A4 proteinP05067Details