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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 (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.

Item Details

Item Type:Refereed Article
Keywords: APP; Heparin binding; Alzheimer's disease; Peptide; Secondary structure
Research Division:Medical and Health Sciences
Research Group:Neurosciences
Research Field:Neurosciences not elsewhere classified
Objective Division:Health
Objective Group:Clinical Health (Organs, Diseases and Abnormal Conditions)
Objective Field:Neurodegenerative Disorders Related to Ageing
Author:Small, DH (Professor David Small)
ID Code:75411
Year Published:1997
Web of Science® Times Cited:43
Deposited By:Research Division
Deposited On:2012-01-30
Last Modified:2012-02-02
Downloads:0

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