Currently, many compounds in clinical trials can prevent fibril formation and aggregation . Researchers are also working on small molecules for this job. For example, Tramiprosate is a molecule that stabilizes the soluble form of amyloid-beta, preventing it from aggregating into fibrils. By mimicking the effects of glycosaminoglycans, Tramiprosate binds to amyloid-beta, reducing its toxicity and aggregation propensity . Another promising small molecule is EGCG (epigallocatechin gallate), a polyphenol found in green tea . EGCG binds to amyloid-beta and inhibits its aggregation into toxic oligomers and fibrils. Amyloid fibrils bind to the plasma membrane through electrostatic interactions, hydrophobic interactions, and specific receptor-ligand binding . The initial attachment often involves electrostatic interactions between the negatively charged membrane components, such as phospholipids and glycosaminoglycans, and the positively charged regions on the fibrils.