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Hydrophobic, aromatic and electrostatic interactions play a central role in amyloid fibril formation

DOI: 10.1021/bi101936c DOI Help

Authors: Karen Marshall (University of Sussex) , Kyle Morris (University of Sussex) , Deborah Charlton (University of Sussex) , Nicola O'reilly (CRUK Peptide Synthesis Laboratory, London Research Institute) , Laurence Lewis (Cancer Research UK London Research Institute) , Helen Walden (London Research Institute of Cancer Research UK) , Louise Serpell (University of Sussex)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Biochemistry , VOL 50 (12)

State: Published (Approved)
Published: February 2011

Abstract: The mechanism by which side chains mediate and modulate amyloid assembly is a pressing question that impacts on both disease related and functionally related amyloid. Amyloid fibrils are characterised by a cross-β structure in which hydrogen bonding is known to provide a means to elongate and polymerise the fibrillar structures. However, side chains impact on the propensity to aggregate and provide a framework by which different morphologies can be formed and the structures can be stabilised via both intersheet and interstrand specific interactions.

Subject Areas: Biology and Bio-materials


Instruments: I24-Microfocus Macromolecular Crystallography