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

Research output: Contribution to journalArticle

230 Citations (Scopus)

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
StatePublished - Aug 1 2003
Externally publishedYes

Fingerprint

Atomic Force Microscopy
Amyloid
Synucleins
Immunoglobulin Light Chains
Proteins
Insulin
Protein Domains

ASJC Scopus subject areas

  • Biophysics

Cite this

Khurana, R., Ionescu-Zanetti, C., Pope, M., Li, J., Nielson, L., Ramirez-Alvarado, M., ... 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.

A general model for amyloid fibril assembly based on morphological studies using atomic force microscopy. / Khurana, Ritu; Ionescu-Zanetti, Cristian; Pope, Maighdlin; Li, Jie; Nielson, Liza; Ramirez-Alvarado, Marina; Regan, Lynn; Fink, Anthony L.; Carter, Sue A.

In: Biophysical Journal, Vol. 85, No. 2, 01.08.2003, p. 1135-1144.

Research output: Contribution to journalArticle

Khurana, R, Ionescu-Zanetti, C, Pope, M, Li, J, Nielson, L, Ramirez-Alvarado, M, Regan, L, Fink, AL & Carter, SA 2003, 'A general model for amyloid fibril assembly based on morphological studies using atomic force microscopy', Biophysical Journal, vol. 85, no. 2, pp. 1135-1144.
Khurana, Ritu ; Ionescu-Zanetti, Cristian ; Pope, Maighdlin ; Li, Jie ; Nielson, Liza ; Ramirez-Alvarado, Marina ; Regan, Lynn ; Fink, Anthony L. ; Carter, Sue A. / A general model for amyloid fibril assembly based on morphological studies using atomic force microscopy. In: Biophysical Journal. 2003 ; Vol. 85, No. 2. pp. 1135-1144.
@article{9560564a47994e789cd05666757d6da4,
title = "A general model for amyloid fibril assembly based on morphological studies using atomic force microscopy",
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.",
author = "Ritu Khurana and Cristian Ionescu-Zanetti and Maighdlin Pope and Jie Li and Liza Nielson and Marina Ramirez-Alvarado and Lynn Regan and Fink, {Anthony L.} and Carter, {Sue A.}",
year = "2003",
month = "8",
day = "1",
language = "English (US)",
volume = "85",
pages = "1135--1144",
journal = "Biophysical Journal",
issn = "0006-3495",
publisher = "Biophysical Society",
number = "2",

}

TY - JOUR

T1 - A general model for amyloid fibril assembly based on morphological studies using atomic force microscopy

AU - Khurana, Ritu

AU - Ionescu-Zanetti, Cristian

AU - Pope, Maighdlin

AU - Li, Jie

AU - Nielson, Liza

AU - Ramirez-Alvarado, Marina

AU - Regan, Lynn

AU - Fink, Anthony L.

AU - Carter, Sue A.

PY - 2003/8/1

Y1 - 2003/8/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0041343061&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0041343061&partnerID=8YFLogxK

M3 - Article

VL - 85

SP - 1135

EP - 1144

JO - Biophysical Journal

JF - Biophysical Journal

SN - 0006-3495

IS - 2

ER -