Makin, O Sumner, Atkins, Edward, Sikorski, Pawel, Johansson, Jan and Serpell, Louise C (2005) Molecular basis for amyloid fibril formation and stability. Proceedings of the National Academy of Sciences, 102 (2). pp. 315-320. ISSN 0027-8424

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Abstract

The molecular structure of the amyloid fibril has remained elusive because of the difficulty of growing well diffracting crystals. By using a sequence-designed polypeptide, we have produced crystals of an amyloid fiber. These crystals diffract to high resolution (1 Å) by electron and x-ray diffraction, enabling us to determine a detailed structure for amyloid. The structure reveals that the polypeptides form fibrous crystals composed of antiparallel ß-sheets in a cross-ß arrangement, characteristic of all amyloid fibers, and allows us to determine the side-chain packing within an amyloid fiber. The antiparallel ß-sheets are zipped together by means of p-bonding between adjacent phenylalanine rings and salt-bridges between charge pairs (glutamic acid¿lysine), thus controlling and stabilizing the structure. These interactions are likely to be important in the formation and stability of other amyloid fibrils.

Item Type:	Article
Additional Information:	Senior Author (LS). First author (student OSM). LS directed the research, wrote the paper and is corresponding author. OSM carried out the research and co-authored the paper. This was the first molecular structure of an amyloid fibril, solved by fibre diffraction and modelling, cited 97 times.
Schools and Departments:	School of Life Sciences > Biochemistry
Depositing User:	Osmar Sumner Makin
Date Deposited:	06 Feb 2012 20:23
Last Modified:	21 May 2012 15:47
URI:	http://sro.sussex.ac.uk/id/eprint/25732

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