Aminocyclodextrin Oligomers as Protective Agents of Protein Aggregation. Issue 7 (7th June 2016)

• Record Type: Journal Article
• Authors: Giglio, Valentina; Bellia, Francesco; Oliveri, Valentina; Vecchio, Graziella
• Is Part Of: ChemPlusChem. Volume 81:Issue 7(2016)
• Page Start: 660
• Page End: 665
• Publication Date: 2016-06-07
• Subjects: amines -- amyloids -- cyclodextrins -- drug carriers -- polymers; Chemistry -- Periodicals; 540.5
• DOI: 10.1002/cplu.201600239
• Languages: English
• ISSNs: 2192-6506

Abstract

Abstract: Over 30 different amyloid proteins and a number of corresponding protein‐misfolding diseases have been identified. Among these is Alzheimer's disease, the most common neurodegenerative disorder. The treatment of these diseases is still a goal to reach and many molecules have been studied in this context. Among these, the cyclodextrins have shown interesting potential as agents against protein aggregation (antiaggregants). On the basis of this interest, we investigated the effect on protein aggregation of some oligomers of β‐cyclodextrins. In particular, it was found that amino oligomers show good inhibition of β‐amyloid aggregation in the micromolar concentration range. The presence of both a multicavity system and amino groups seems to be essential for preventing protein aggregation. Abstract : Keep away from each other ! Aminocyclodextrin oligomers were synthesized and their ability to inhibit the aggregation of amyloid proteins was compared to that of unfunctionalized oligomers or polymers. Aggregation of Aβ protein was inhibited at micromolar concentrations, and significantly, the oligomers were not cytotoxic. The presence of both a multicavity system and amino groups seems to have a key role in the antiaggregant activity.