A general model for amyloid fibril assembly based on morphological studies using atomic force microscopy

Ritu Khurana, Cristian Ionescu-Zanetti, Maighdlin Pope, Jie Li, Liza Nielson, Marina Ramirez-Alvarado, Lynn Regan, Anthony L. Fink, Sue A. Carter

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Abstract

Based on atomic force microscopy analysis of the morphology of fibrillar species formed during fibrillation of α-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.

Original languageEnglish (US)
Pages (from-to)1135-1144
Number of pages10
JournalBiophysical Journal
Volume85
Issue number2
DOIs
StatePublished - Aug 1 2003

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ASJC Scopus subject areas

  • Biophysics

Cite this

Khurana, R., Ionescu-Zanetti, C., Pope, M., Li, J., Nielson, L., Ramirez-Alvarado, M., Regan, L., Fink, A. L., & Carter, S. A. (2003). A general model for amyloid fibril assembly based on morphological studies using atomic force microscopy. Biophysical Journal, 85(2), 1135-1144. https://doi.org/10.1016/S0006-3495(03)74550-0