| Beta-Amyloid (1-40) (Abeta40) is an aggregation prone protein, which undergoes a nucleation-dependent aggregation process causing the pathological neurodegeneration by amyloid plaque formation implicated in Alzheimer's disease. In this thesis, we investigated the effects of small molecule modulators extracted from the marine invertebrate Pseudopterogorgia elisabethae on the Abeta40 amyloidogenic process using in-vitro ThT fluorescence assay and atomic force microscopy. We also investigated the effects of neutral and anionic phospholipid liposomes on Abeta40 aggregation. Our results show that a marine natural product Pseudopterosin-A and its derivatives can suppress and modulate the Abeta40 aggregation process. Furthermore, our results demonstrate that a neutral phospholipid liposome inhibits Abeta40 fibril formation, whereas the anionic liposomes promote it. |
