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Expression and analysis of heparin-binding regions of the amyloid precursor protein of Alzheimer's disease
Citation
Mok, SS and Sberna, G and Heffernan, D and Cappai, R and Galatis, D and Clarris, HJ and Sawyer, WH and Beyreuther, K and Masters, CL and Small, DH, Expression and analysis of heparin-binding regions of the amyloid precursor protein of Alzheimer's disease, F E B S Letters: (Federation of European Biochemical Societies), 415, (3) pp. 303-307. ISSN 0014-5793 (1997) [Refereed Article]
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DOI: doi:10.1016/S0014-5793(97)01146-0
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 (APP316â€"447) was further characterised by binding studies with peptides encompassing this region. Peptides homologous to APP316â€"346 and APP416â€"447 were found to bind heparin. Circular dichroism studies show that APP416â€"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.
Item Details
Item Type: | Refereed Article |
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Keywords: | APP; Heparin binding; Alzheimer's disease; Peptide; Secondary structure |
Research Division: | Biomedical and Clinical Sciences |
Research Group: | Neurosciences |
Research Field: | Neurosciences not elsewhere classified |
Objective Division: | Health |
Objective Group: | Clinical health |
Objective Field: | Clinical health not elsewhere classified |
UTAS Author: | Small, DH (Professor David Small) |
ID Code: | 75411 |
Year Published: | 1997 |
Web of Science® Times Cited: | 50 |
Deposited By: | Research Division |
Deposited On: | 2012-01-30 |
Last Modified: | 2012-02-02 |
Downloads: | 0 |
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