Taylor, Mark and Moore, Susan and Mourtas, Spyridon and Niarakis, Anna and Re, Francesca and Zona, Cristiano and La Ferla, Barbara and Nicotra, Francesco and Masserini, Massimo and Antimisiaris, Sophia G and Gregori, Maria and Allsop, David (2011) Effect of curcumin-associated and lipid ligand-functionalized nanoliposomes on aggregation of the Alzheimer's Aβ peptide. Nanomedicine: Nanotechnology, Biology, and Medicine, 7 (5). pp. 541-550.Full text not available from this repository.
The effect of various types of nanoliposomes (associated with curcumin, phosphatidic acid, cardiolipin, or GM1 ganglioside) on the aggregation of the amyloid-β(1-42) (Aβ(1-42)) peptide was investigated. Nanoliposomes incorporating curcumin (curcumin-liposomes) were prepared by adding curcumin in the lipid phase during liposome preparation, whereas curcumin surface-decorated liposomes were prepared by using a curcumin-lipid conjugate (lipid-S-curcumin liposomes) or by attaching a curcumin derivative on preformed liposomes by click chemistry (click-curcumin liposomes). The lipid ligands (phosphatidic acid, cardiolipin, or GM1) were also incorporated into nanoliposomes during their formation. All nanoliposomes with curcumin, or the curcumin derivative, were able to inhibit the formation of fibrillar and/or oligomeric Aβ in vitro. Of the three forms of curcumin liposomes tested, the click-curcumin type was by far the most effective. Liposomes with lipid ligands only inhibited Aβ fibril and oligomer formation at a very high ratio of liposome to peptide. Curcumin-based liposomes could be further developed as a novel treatment for Alzheimer's disease.
|Journal or Publication Title:||Nanomedicine: Nanotechnology, Biology, and Medicine|
|Additional Information:||Copyright © 2011 Elsevier Inc. All rights reserved.|
|Uncontrolled Keywords:||Liposomes ; Curcumin ; Amyloid-β ; Oligomer ; Fibril|
|Departments:||Faculty of Health and Medicine > Biomedical & Life Sciences|
|Deposited On:||07 Nov 2011 09:42|
|Last Modified:||25 Feb 2017 02:50|
Actions (login required)