@article {49049,
	title = {Physical basis of amyloid fibril polymorphism.},
	journal = {Nature Communications},
	volume = {9},
	year = {2018},
	month = {2018 Feb 16},
	pages = {699},
	abstract = {<p>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.</p>
},
	issn = {2041-1723},
	doi = {10.1038/s41467-018-03164-5},
	author = {Close, William and Neumann, Matthias and Schmidt, Andreas and Hora, Manuel and Annamalai, Karthikeyan and Schmidt, Matthias and Reif, Bernd and Schmidt, Volker and Grigorieff, Nikolaus and F{\"a}ndrich, Marcus}
}
@article {47506,
	title = {Cryo-EM reveals the steric zipper structure of a light chain-derived amyloid fibril.},
	journal = {Proceedings of the National Academy of Sciences of the United States of America},
	volume = {113},
	year = {2016},
	month = {2016 May 16},
	pages = {6200-5},
	abstract = {<p>Amyloid fibrils are proteinaceous aggregates associated with diseases in humans and animals. The fibrils are defined by intermolecular interactions between the fibril-forming polypeptide chains, but it has so far remained difficult to reveal the assembly of the peptide subunits in a full-scale fibril. Using electron cryomicroscopy (cryo-EM), we present a reconstruction of a fibril formed from the pathogenic core of an amyloidogenic immunoglobulin (Ig) light chain. The fibril density shows a lattice-like assembly of face-to-face packed peptide dimers that corresponds to the structure of steric zippers in peptide crystals. Interpretation of the density map with a molecular model enabled us to identify the intermolecular interactions between the peptides and rationalize the hierarchical structure of the fibril based on simple chemical principles.</p>
},
	issn = {1091-6490},
	doi = {10.1073/pnas.1522282113},
	author = {Schmidt, Andreas and Annamalai, Karthikeyan and Schmidt, Matthias and Grigorieff, Nikolaus and F{\"a}ndrich, Marcus}
}
