Human amylin is a potent antimicrobial peptide that exhibits antimicrobial synergism with the amyloid beta protein.

Introduction: Our previous studies demonstrated the antimicrobial properties of amyloid beta (Aβ) of Alzheimer's disease (AD) against clinically relevant bacteria, yeast, and viruses. In this study, we investigate the antimicrobial function of the 37-amino acid amylin of type 2 diabetes (T2D), expanding on its potential involvement in AD.

Methods: We used in vitro assays, including human three-dimensional neuronal cell culture models, to test microbicidal, microbiostatic, and synergistic antimicrobial interactions between amylin and Aβ against microbes.

Alzheimer's Pathogenesis, Metal-Mediated Redox Stress, and Potential Nanotheranostics.

Alzheimer's disease (AD) characterized by insoluble amyloid-β (Aβ) deposits, neurofibrillary tangles (NFTs), and neuronal demise. The influence of environmental and genetic factors on AD progression remains elusive, however evidence suggests biometal dyshomeostasis elicits neuronal death, neuroinflammation, and accumulated oxidative damages in AD brain. As such, three pathways have been identified that result from abnormal biometal accumulation and increased levels of reactive oxygen species (ROS) and reactive nitrogen species (RNS) in AD brain parenchyma: (1) the damage caused by direct oxidation of cellular components such as DNA and proteins; (2) the oligomerization of Aβ and NFTs, and (3) the promotion of apoptosis through NF-κB signaling pathway.