Please use this identifier to cite or link to this item:
https://libjncir.jncasr.ac.in/xmlui/handle/10572/56
Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Sanghamitra, Nusrat J M | - |
dc.contributor.author | Varghese, Neenu | - |
dc.contributor.author | Rao, C N R | - |
dc.date.accessioned | 2011-03-04T06:13:29Z | - |
dc.date.available | 2011-03-04T06:13:29Z | - |
dc.date.issued | 2010-08-20 | - |
dc.identifier | 0009-2614 | en_US |
dc.identifier.citation | Chemical Physics Letters 496(1-3), 104–108 (2010) | en_US |
dc.identifier.uri | https://libjncir.jncasr.ac.in/xmlui/10572/56 | - |
dc.description | Restricted access. | en_US |
dc.description.abstract | Characteristic features of a perilous neuro-degenerative disease such as the Alzhiemer's disease is fibrillar plaque formation by the amyloid (A beta) peptide. We have modelled the formation and disintegration of fibrils by studying the aggregate structures formed by A beta structural motif diphenylalanine as well as insulin and bovine serum albumin at the organic aqueous interface. Even small concentrations of curcumin in the organic medium or Cu2+ and Zn2+ ions in the aqueous medium are found to break down the fibrillar structures. (C) 2010 Elsevier B.V. All rights reserved. | en_US |
dc.description.uri | http://dx.doi.org/10.1016/j.cplett.2010.07.017 | en_US |
dc.language.iso | en | en_US |
dc.publisher | Elsevier BV | en_US |
dc.rights | © 2010 Elsevier BV | en_US |
dc.subject | Beta Peptide | en_US |
dc.subject | In-Vivo | en_US |
dc.subject | A-Beta | en_US |
dc.subject | Nanotubes | en_US |
dc.subject | Diphenylalanine | en_US |
dc.subject | Nanostructures | en_US |
dc.subject | Biosynthesis | en_US |
dc.subject | Plaques | en_US |
dc.subject | Zinc | en_US |
dc.title | Effect of curcumin and Cu2+/Zn2+ ions on the fibrillar aggregates formed by the amyloid peptide and other peptides at the organic–aqueous interface | en_US |
dc.type | Article | en_US |
Appears in Collections: | Research Papers (Prof. C.N.R. Rao) |
Files in This Item:
File | Description | Size | Format | |
---|---|---|---|---|
Sl.No.3 Elsevier.pdf Restricted Access | 860.15 kB | Adobe PDF | View/Open Request a copy |
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.