Curcumin-Like Compounds as Neuroprotective Agents: Interactions with HSP60 and Amyloid Beta Peptide

Alzheimer’s Disease (AD) represents a fundamental challenge for public health in the 21st century. Current AD therapies largely focus on symptomatic aspects of the clinical pathology, but they have yet to demonstrate any major impact on the disease progression [1]. The most important role of the research aimed at fighting the AD is the development of neuro-protective agents, able to interfere with the protein aggregation process whose clinical signature is represented by the plaques deposition. An important role in AD’s framework could be played by Heat shock proteins (HSPs), highly regulated proteins that mediate the proteins proper folding and promote recovery of their native conformation…

Effect of Total Apple Polyphenols Extract as Inhibitors of Amyloid Protein Aggregation

Effect of Total Apple Polyphenols Extract as Inhibitors of Amyloid Protein Aggregation By: Guarrasi, Valeria; Rappa, Cinzia Giacoma; Costa, Maria Assunta; et al. JOURNAL OF CLINICAL GASTROENTEROLOGY Volume: 52 Supplement: 1 Pages: S94-S94 Published: NOV-DEC 2018

Naïve Hsp60, similarly to GroEL, oligomerizes to build heptameric and tetradecameric structures.

Entrapment of Aβ(1-40) peptide in unstructured aggregates

Recognizing the complexity of the fibrillogenesis process provides a solid ground for the development of therapeutic strategies aimed at preventing or inhibiting protein-protein aggregation. Under this perspective, it is meaningful to identify the possible aggregation pathways and their relative products. We found that Aβ-peptide dissolved in a pH 7.4 solution at small peptide concentration and low ionic strength forms globular aggregates without typical amyloid β-conformation. ThT binding kinetics was used to monitor aggregate formation. Circular dichroism spectroscopy, AFM imaging, static and dynamic light scattering were used for structural and morphological characterization of the aggre…