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

Overview

Journal Biophys J

Publisher Cell Press

Specialty Biophysics

Date 2003 Jul 30

PMID 12885658

Citations 83

Authors

Ritu Khurana

Cristian Ionescu-Zanetti

Maighdlin Pope

Jie Li

Liza Nielson

Marina Ramirez-Alvarado

Lynn Regan

Anthony L Fink

Sue A Carter

Affiliations

Soon will be listed here.

Abstract

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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