TAILIEUCHUNG - Báo cáo khoa học: Mechanisms of amyloid fibril formation – focus on domain-swapping

Conformational diseases constitute a group of heterologous disorders in which a constituent host protein undergoes changes in conformation, lead-ing to aggregation and deposition. To understand the molecular mecha-nisms of the process of amyloid fibril formation, numerousin vitro and in vivo studies, including model and pathologically relevant proteins, have been performed. | IFEBS Journal REVIEW ARTICLE Mechanisms of amyloid fibril formation - focus on domain-swapping Eva Zerovnik1 Veronika Stoka1 Andreja Mirtic2 Gregor Guncar3 Joze Grdadolnik2 4 Rosemary A. Staniforth5 Dusan Turk1 6 and Vito Turk1 1 Department of Biochemistry and Molecular and StructuralBiology Jozef Stefan Institute Ljubljana Slovenia 2 Laboratory of Biomolecular Structure NationalInstitute of Chemistry Ljubljana Slovenia 3 Department of Biochemistry Faculty of Chemistry and ChemicalTechnology University of Ljubljana Slovenia 4 En-Fist Centre of Excellence Ljubljana Slovenia 5 Department of Molecular Biology and Biotechnology University of Sheffield UK 6 Center of Excellence for Integrated Approaches in Chemistry and Biology of Proteins Ljubljana Slovenia Keywords domain-swapping mechanisms of amyloid-fibrilformation protein aggregation stefin B toxic oligomers Correspondence E. Zerovnik Department of Biochemistry and Molecular and StructuralBiology JoZef Stefan Institute Jamova 39 1000 Ljubljana Slovenia Fax 386 1 477 3984 Tel 386 1 477 3753 E-mail Received 18 February 2011 revised 6 April 2011 accepted 28 April 2011 Conformational diseases constitute a group of heterologous disorders in which a constituent host protein undergoes changes in conformation leading to aggregation and deposition. To understand the molecular mechanisms of the process of amyloid fibril formation numerous in vitro and in vivo studies including model and pathologically relevant proteins have been performed. Understanding the molecular details of these processes is of major importance to understand neurodegenerative diseases and could contribute to more effective therapies. Many models have been proposed to describe the mechanism by which proteins undergo ordered aggregation into amyloid fibrils. We classify these as a templating and nucleation b linear colloid-like assembly of spherical oligomers and c domain-swapping. In this review we stress the role of domain-swapping

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