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Expression and analysis of heparin‐binding regions of the amyloid precursor protein of Alzheimer's disease
Author(s) -
Mok Su San,
Sberna Gian,
Heffernan Damien,
Cappai Roberto,
Galatis Denise,
Clarris Heidi J,
Sawyer William H,
Beyreuther Konrad,
Masters Colin L,
Small David H
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01146-0
Subject(s) - heparin , alzheimer's disease , chemistry , amyloid (mycology) , disease , p3 peptide , amyloid precursor protein , biochemistry , amyloid β , microbiology and biotechnology , medicine , biology , inorganic chemistry
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.