Amyloid fibrils are a special class of self-assembled protein molecules, which exhibit
various toxic effects in cells. Different physiological disorders such as Alzheimer’s, Parkinson’s,
Huntington’s diseases, etc. happen due to amyloid formation and lack of proper cellular mechanism
for the removal of fibrils. Therefore, inhibition of amyloid fibrillation will find immense
applications to combat the diseases associated with amyloidosis. The development of therapeutics
against amyloidosis is definitely challenging and numerous strategies have been followed to find
out anti-amyloidogenic molecules. Inhibition of amyloid aggregation of proteins can be achieved
either by stabilizing the native conformation or by decreasing the chances of assembly formation by
the unfolded/misfolded structures. Various small molecules such as naturally occurring
polyphenols, flavonoids, small organic molecules, surfactants, dyes, chaperones, etc. have
demonstrated their capability to interrupt the amyloid fibrillation of proteins. In addition to that, in
last few years, different nanomaterials were evolved as effective therapeutic inhibitors against
amyloidosis. Aromatic and hydrophobic interactions between the partially unfolded protein
molecules and the inhibitors had been pointed as a general mechanism for inhibition. In this review
article, we are presenting an overview on the inhibition of amyloidosis by using different small
molecules (both natural and synthetic origin) as well as nanomaterials for development of
pharmaceutical strategies against amyloid diseases.
Slow Dissolution Kinetics of Model Peptide Fibrils
