Conformational stability of Abeta-(25-35) in the presence of thiazolidine derivatives.
In the attempt to identify a new lead compound able to modify the conformational preferences of the beta-amyloid peptides, a set of new compounds characterized by a thiazolidine ring linked to several different aryl moieties were synthesized. The ability of these compounds to prevent the beta-amyloid aggregation was evaluated using circular dichroism and nuclear magnetic resonance techniques. Molecular docking procedure allowed an interpretation of spectroscopic in the key of molecular interaction.
Campiglia
Pietro
P
Dipartimento di Scienze Farmaceutiche, University of Salerno, 84084 Fisciano, Italy.
Esposito
Cinzia
C
Scrima
Mario
M
Gomez-Monterrey
Isabel
I
Bertamino
Alessia
A
Grieco
Paolo
P
Novellino
Ettore
E
D'Ursi
Anna Maria
AM
D016229:Amyloid beta-Peptides / Q000737:chemistry*; D002942:Circular Dichroism; D006801:Humans; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary; D053778:Thiazolidines / Q000138:chemical synthesis / Q000737:chemistry*
D016229:Amyloid beta-Peptides; D010455:Peptides; D053778:Thiazolidines