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TitlePhysical basis of amyloid fibril polymorphism.
Journal, issue, pagesNat Commun, Vol. 9, Issue 1, Page 699, Year 2018
Publish dateFeb 16, 2018
AuthorsWilliam Close / Matthias Neumann / Andreas Schmidt / Manuel Hora / Karthikeyan Annamalai / Matthias Schmidt / Bernd Reif / Volker Schmidt / Nikolaus Grigorieff / Marcus Fändrich /
PubMed AbstractPolymorphism is a key feature of amyloid fibril structures but it remains challenging to explain these variations for a particular sample. Here, we report electron cryomicroscopy-based ...Polymorphism is a key feature of amyloid fibril structures but it remains challenging to explain these variations for a particular sample. Here, we report electron cryomicroscopy-based reconstructions from different fibril morphologies formed by a peptide fragment from an amyloidogenic immunoglobulin light chain. The observed fibril morphologies vary in the number and cross-sectional arrangement of a structurally conserved building block. A comparison with the theoretically possible constellations reveals the experimentally observed spectrum of fibril morphologies to be governed by opposing sets of forces that primarily arise from the β-sheet twist, as well as peptide-peptide interactions within the fibril cross-section. Our results provide a framework for rationalizing and predicting the structure and polymorphism of cross-β fibrils, and suggest that a small number of physical parameters control the observed fibril architectures.
External linksNat Commun / PubMed:29453354 / PubMed Central
MethodsEM (helical sym.)
Resolution8.4 - 20.3 Å
Structure data

EMDB-3986:
Morphology II - cross-beta amyloid fibril structure from the IGSNVVTWYQQL peptide of AL immunoglobulin light chain by cryo-EM
Method: EM (helical sym.) / Resolution: 8.4 Å

EMDB-3987:
Morphology III - cross-beta amyloid fibril structure from the IGSNVVTWYQQL peptide of AL immunoglobulin light chain by cryo-EM
Method: EM (helical sym.) / Resolution: 9.3 Å

EMDB-3988:
Morphology IV - cross-beta amyloid fibril structure from the IGSNVVTWYQQL peptide of AL immunoglobulin light chain by cryo-EM
Method: EM (helical sym.) / Resolution: 9.7 Å

EMDB-3989:
Morphology V - cross-beta amyloid fibril structure from the IGSNVVTWYQQL peptide of AL immunoglobulin light chain by cryo-EM
Method: EM (helical sym.) / Resolution: 9.4 Å

EMDB-3990:
Morphology VI - cross-beta amyloid fibril structure from the IGSNVVTWYQQL peptide of AL immunoglobulin light chain by cryo-EM
Method: EM (helical sym.) / Resolution: 13.4 Å

EMDB-3991:
Morphology VII - cross-beta amyloid fibril structure from the IGSNVVTWYQQL peptide of AL immunoglobulin light chain by cryo-EM
Method: EM (helical sym.) / Resolution: 15.9 Å

EMDB-3992:
Morphology VIII - cross-beta amyloid fibril structure from the IGSNVVTWYQQL peptide of AL immunoglobulin light chain by cryo-EM
Method: EM (helical sym.) / Resolution: 18.2 Å

EMDB-3993:
Morphology IX - cross-beta amyloid fibril structure from the IGSNVVTWYQQL peptide of AL immunoglobulin light chain by cryo-EM
Method: EM (helical sym.) / Resolution: 20.3 Å

EMDB-3994:
Morphology X - cross-beta amyloid fibril structure from the IGSNVVTWYQQL peptide of AL immunoglobulin light chain by cryo-EM
Method: EM (helical sym.) / Resolution: 17.7 Å

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  • Homo sapiens (human)

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