Premium
Porphyrin Cyclodextrin Conjugates Modulate Amyloid Beta Peptide Aggregation and Cytotoxicity
Author(s) -
Oliveri Valentina,
Zimbone Stefania,
Giuffrida Maria Laura,
Bellia Francesco,
Tomasello Marianna Flora,
Vecchio Graziella
Publication year - 2018
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201800807
Subject(s) - cytotoxicity , chemistry , cyclodextrin , peptide , porphyrin , conjugate , amyloid (mycology) , amyloid beta , small molecule , biophysics , toxicity , biochemistry , combinatorial chemistry , in vitro , biology , organic chemistry , inorganic chemistry , mathematical analysis , mathematics
Although fibrillar amyloid beta peptide (Aβ) aggregates are one of the major hallmarks of Alzheimer's disease, increasing evidence suggests that soluble Aβ oligomers are the primary toxic species. Targeting the oligomeric species could represent an effective strategy to interfere with Aβ toxicity. In this work, the biological properties of 5[4‐(6‐O‐β‐cyclodextrin)‐phenyl],10,15,20‐tri(4‐hydroxyphenyl)‐porphyrin and its zinc complex were tested, as new molecules that interact with Aβ and effectively prevent its cytotoxicity. We found that these systems can cross the cell membrane to deliver Aβ intracellularly and promote its clearance. Our results provide evidence for the use of cyclodextrin–porphyrin derivatives as a promising strategy to target amyloid aggregation.