Multicomponent, fragment-based synthesis of polyphenol-containing peptidomimetics and their inhibiting activity on beta-amyloid oligomerization. Issue 44 (31st October 2017)

• Record Type: Journal Article
• Authors: Lambruschini, Chiara; Galante, Denise; Moni, Lisa; Ferraro, Francesco; Gancia, Giulio; Riva, Renata; Traverso, Alessia; Banfi, Luca; D'Arrigo, Cristina
• Is Part Of: Organic & biomolecular chemistry. Volume 15:Issue 44(2017)
• Page Start: 9331
• Page End: 9351
• Publication Date: 2017-10-31
• Subjects: Chemistry, Organic -- Periodicals; Bioorganic chemistry -- Periodicals; Chemistry, Physical organic -- Periodicals; 547
• DOI: 10.1039/c7ob02182h
• Languages: English
• ISSNs: 1477-0520

Abstract

Abstract : A new and short fragment-based approach towards artificial (but "natural-based") complex polyphenols has been developed, exploiting the Ugi multicomponent reaction of phenol-containing simple substrates. Abstract : A new and short fragment-based approach towards artificial (but "natural-based") complex polyphenols has been developed, exploiting the Ugi multicomponent reaction of phenol-containing simple substrates. The resulting library of compounds has been tested for its capacity to inhibit β-amyloid protein aggregation, as a possible strategy to develop new chemical entities to be used as prevention or therapy for Alzheimer's disease. Some of the members of this library have demonstrated, in thioflavin assays, a highly promising activity in inhibiting aggregation for two β-amyloid peptides: Aβ1-42 and the truncated AβpE3-42.