TAILIEUCHUNG - Báo cáo khoa học: Understanding the complex mechanisms of b2-microglobulin amyloid assembly

Several protein misfolding diseases are associated with the conversion of native proteins into ordered protein aggregates known as amyloid. Studies of amyloid assemblies have indicated that non-native proteins are responsi-ble for initiating aggregationin vitro andin vivo. | IFEBS Journal REVIEW ARTICLE Understanding the complex mechanisms of b2-microglobulin amyloid assembly Timo Eichner1 2 and Sheena E. Radford2 1 Department of Biochemistry Brandeis University Waltham MA USA 2 Astbury Centre for StructuralMolecular Biology and Institute of Molecular Cellular Biology University of Leeds UK Keywords amyloid conformationalconversion dialysis-related amyloidosis dynamics NMR prion Correspondence S. E. Radford Astbury Centre for Structural Molecular Biology and Institute of Molecular Cellular Biology University of Leeds Leeds LS2 9JT UK Fax 44 113 343 7486 Tel 44 113 343 3170 E-mail T. Eichner Department of Biochemistry Brandeis University Waltham MA 02454 USA Fax 1 781 736 2316 Tel 1 781 736 2326 E-mail teichner@ Several protein misfolding diseases are associated with the conversion of native proteins into ordered protein aggregates known as amyloid. Studies of amyloid assemblies have indicated that non-native proteins are responsible for initiating aggregation in vitro and in vivo. Despite the importance of these species for understanding amyloid disease the structural and dynamic features of amyloidogenic intermediates and the molecular details of how they aggregate remain elusive. This review focuses on recent advances in developing a molecular description of the folding and aggregation mechanisms of the human amyloidogenic protein b2-microglobulin under physiologically relevant conditions. In particular the structural and dynamic properties of the non-native folding intermediate IT and its role in the initiation of fibrillation and the development of dialysis-related amyloidosis are discussed. Re-use of this article is permitted in accordance with the Terms and Conditions set out at http onlineopen OnlineOpen_Terms Received 5 April 2011 revised 11 May 2011 accepted 13 May 2011 doi The role of b2-microglobulin in amyloid disease .

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