dc.contributor.author |
Harris, Paul |
en |
dc.contributor.author |
Squire, Christopher |
en |
dc.contributor.author |
Young, PG |
en |
dc.contributor.author |
Brimble, Margaret |
en |
dc.date.accessioned |
2016-08-05T01:56:06Z |
en |
dc.date.issued |
2015-01 |
en |
dc.identifier.citation |
Biopolymers (Peptid Science), 2015, 104 (1), pp. 37 - 45 |
en |
dc.identifier.issn |
0006-3525 |
en |
dc.identifier.uri |
http://hdl.handle.net/2292/29814 |
en |
dc.description.abstract |
The chemical synthesis of analogue of a novel γ-secretase activating protein, which may play a pivotal role in the formation of amyloid peptides, the precursor to Alzheimer's disease, is described. The linear polypeptide sequence, consisting of 121 amino acids was assembled from four unprotected peptide building blocks using a convergent ligation-based synthesis. A strategic mutation of three glutamine residues to cysteine enabled the ligations, and the cysteines were subsequently converted to pseudoglutamines, to mimic the native glutamine. The full length unfolded protein was obtained in milligram amounts and was demonstrated to be homogeneous by liquid chromatography and mass spectrometry. |
en |
dc.description.uri |
http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1097-0282a |
en |
dc.publisher |
Wiley |
en |
dc.relation.ispartofseries |
Biopolymers (Peptid Science) |
en |
dc.rights |
Items in ResearchSpace are protected by copyright, with all rights reserved, unless otherwise indicated. Previously published items are made available in accordance with the copyright policy of the publisher. Details obtained from http://www.sherpa.ac.uk/romeo/issn/0006-3525/ |
en |
dc.rights.uri |
https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm |
en |
dc.subject |
Glutamine |
en |
dc.subject |
Peptide Fragments |
en |
dc.subject |
Ligation |
en |
dc.subject |
Amyloid Precursor Protein Secretases |
en |
dc.subject |
Amyloid beta-Peptides |
en |
dc.title |
Chemical synthesis of γ-secretase activating protein using pseudoglutamines as ligation sites |
en |
dc.type |
Journal Article |
en |
dc.identifier.doi |
10.1002/bip.22600 |
en |
pubs.issue |
1 |
en |
pubs.begin-page |
37 |
en |
pubs.volume |
104 |
en |
dc.rights.holder |
Copyright:
Wiley |
en |
dc.identifier.pmid |
25523549 |
en |
pubs.author-url |
http://onlinelibrary.wiley.com/doi/10.1002/bip.22600/full |
en |
pubs.end-page |
45 |
en |
pubs.publication-status |
Published |
en |
dc.rights.accessrights |
http://purl.org/eprint/accessRights/RestrictedAccess |
en |
pubs.subtype |
Article |
en |
pubs.elements-id |
471262 |
en |
pubs.org-id |
Science |
en |
pubs.org-id |
Biological Sciences |
en |
pubs.org-id |
Chemistry |
en |
pubs.org-id |
Science Research |
en |
pubs.org-id |
Maurice Wilkins Centre (2010-2014) |
en |
dc.identifier.eissn |
1097-0282 |
en |
pubs.record-created-at-source-date |
2016-08-05 |
en |
pubs.dimensions-id |
25523549 |
en |