TAILIEUCHUNG - Báo cáo khoa học: Mechanisms of amyloid fibril self-assembly and inhibition Model short peptides as a key research tool

The formation of amyloid fibrils is associated with various human medical disorders of unrelated origin. Recent research indicates that self-assembled amyloid fibrils are also involved in physiological processes in several micro-organisms. Yet, the molecular basis for the recognition and self-assembly processes mediating the formation of such structures from their soluble protein precursors is not fully understood. | ềFEBS Journal MINIREVIEW Mechanisms of amyloid fibril self-assembly and inhibition Model short peptides as a key research tool Ehud Gazit Department of Molecular Microbiology and Biotechnology TelAviv University TelAviv Israel Keywords amyloid formation molecular recognition protein folding protein misfolding proteinprotein interactions self-assembly stacking interactions Correspondence E. Gazit Department of Molecular Microbiology and Biotechnology TelAviv University TelAviv 69978 Israel Fax 972 3 640 5448 Tel 972 3 640 9030 E-mail ehudg@ Received 2 June 2005 accepted 10 October 2005 doi The formation of amyloid fibrils is associated with various human medical disorders of unrelated origin. Recent research indicates that self-assembled amyloid fibrils are also involved in physiological processes in several microorganisms. Yet the molecular basis for the recognition and self-assembly processes mediating the formation of such structures from their soluble protein precursors is not fully understood. Short peptide models have provided novel insight into the mechanistic issues of amyloid formation revealing that very short peptides as short as a tetrapeptide contain all the necessary molecular information for forming typical amyloid fibrils. A careful analysis of short peptides has not only facilitated the identification of molecular recognition modules that promote the interaction and selfassembly of fibrils but also revealed that aromatic interactions are important in many cases of amyloid formation. The realization of the role of aromatic moieties in fibril formation is currently being used to develop novel inhibitors that can serve as therapeutic agents to treat amyloid-associated disorders. The formation of well-ordered amyloid fibrils by the self-assembly of various proteins and polypeptides is associated with serious human medical disorders like Alzheimer s disease prion disorders bovine spongiform encephalopathy .

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