Polyallylamine Binds to Aβ Amyloid and Inhibits Antibody Recognition.

Protein amyloids have attracted attention for their application as functional amyloid materials because of their strong properties, such as high resistance to chemical or biological degradation, despite their medical issues. Amyloids can be used for various applications by modifying the amyloid surface with functional materials, such as proteins and polymers. In this study, we investigated the effect of polyallylamine (PAA), a functional cationic polymer as a candidate for amyloid modification, on the amyloids formed from amyloid β (Aβ) peptide.

Peroxynitric acid inhibits amyloid β aggregation.

Peroxynitric acid (PNA), a reactive oxygen nitrogen species, has attracted attention in life science because of its unique properties such as high bacteriacidal activity. Since the bactericidal activity of PNA could be related to its reaction with amino acid residues, we speculate that PNA can be used for protein modifications. In this study, PNA was applied to inhibit aggregation of amyloid β1-42 (Aβ42), which is thought to cause Alzheimer's disease (AD).

Inhibition of amyloid formation of amyloid β (1-42), amylin and insulin by 1,5-diazacyclooctanes, a spermine-acrolein conjugate.

Amyloid aggregates of proteins are known to be involved in various diseases such as Alzheimer's disease (AD). It is therefore speculated that the inhibition of amyloid formation can play an important role in the prevention of various diseases involving amyloids. Recently, we have found that acrolein reacts with polyamines, such as spermine, and produces 1,5-diazacyclooctane, such as cyclic spermine (cSPM).