Can deposition of amyloid be prevented in Alzheimer's disease?

Amyloid is a generic term referring to extracellular fibrillar protein deposits defined by their unique tinctorial, ultrastructural, and protein conformational properties. At least 17 different forms have been identified. In each form the deposit consists of a disease-specific (or pathologic process-specific) protein and a set of common components. The disease-specific protein serves as the basis for the classification of the amyloids. In inflammation-associated (AA) amyloid it can be demonstrated that interactive processes between serum amyloid A (SAA), the AA precursor, and the common components, are likely responsible for AA amyloid deposition. Understanding the details of these interactions provide targets for therapeutic interference that are successful in vivo. Analogous interactions take place between the common components and the beta-protein and beta-protein precursor responsible for the congophilic angiopathy and neuritic plaque amyloid in Alzheimer's disease. Interference with beta-protein/common component interaction in vitro both prevents and reverses beta-protein fibril assembly, indicating that successful delivery of effective agents across the blood-brain barrier should prevent and possibly reverse amyloid deposition in Alzheimer's disease.