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Biophysical Journal 85:1135-1144 (2003)
© 2003 The Biophysical Society

A General Model for Amyloid Fibril Assembly Based on Morphological Studies Using Atomic Force Microscopy

Ritu Khurana *, Cristian Ionescu-Zanetti {dagger}, Maighdlin Pope {dagger}, Jie Li *, Liza Nielson *, Marina Ramírez-Alvarado {ddagger}, Lynn Regan {ddagger}, Anthony L. Fink * and Sue A. Carter {dagger}

Departments of * Chemistry and Biochemistry and {dagger} Physics, University of California at Santa Cruz, Santa Cruz, California 95064; and {ddagger} Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520-8114

Correspondence: Address reprint requests to Ritu Khurana, Molecular and Structural Biology Division, Central Drug Research Institute, Lucknow 226001, India. E-mail: ritukhurana2001{at}yahoo.com or Sue A. Carter, Dept. of Physics, University of California at Santa Cruz, Santa Cruz, CA 95064. E-mail: sacarter{at}cats.ucsc.edu.

Based on atomic force microscopy analysis of the morphology of fibrillar species formed during fibrillation of {alpha}-synuclein, insulin, and the B1 domain of protein G, a previously described model for the assembly of amyloid fibrils of immunoglobulin light-chain variable domains is proposed as a general model for the assembly of protein fibrils. For all of the proteins studied, we observed two or three fibrillar species that vary in diameter. The smallest, protofilaments, have a uniform height, whereas the larger species, protofibrils and fibrils, have morphologies that are indicative of multiple protofilaments intertwining. In all cases, protofilaments intertwine to form protofibrils, and protofibrils intertwine to form fibrils. We propose that the hierarchical assembly model describes a general mechanism of assembly for all amyloid fibrils.




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