Issue 10, 2011

An amyloid-like fibril-forming supramolecular cross-β-structure of a model peptide: a crystallographic insight

Abstract

The peptideBoc-Val-Phe-OMe 1 bearing sequence similarity with the central hydrophobic cluster (CHC) of Alzheimer's Aβ18-19peptide self-assembles to produce amyloid-like straight unbranched fibrils as examined by atomic force microscopy and Congo red assay. Single crystal X-ray diffraction offers the atomic level structure of the supramolecular parallel β-sheet aggregation and antiparallel separation between layers (cross-β-structure).

Graphical abstract: An amyloid-like fibril-forming supramolecular cross-β-structure of a model peptide: a crystallographic insight

Supplementary files

Article information

Article type
Paper
Submitted
16 Nov 2010
Accepted
18 Feb 2011
First published
23 Feb 2011

Org. Biomol. Chem., 2011,9, 3787-3791

An amyloid-like fibril-forming supramolecular cross-β-structure of a model peptide: a crystallographic insight

S. Maity, P. Kumar and D. Haldar, Org. Biomol. Chem., 2011, 9, 3787 DOI: 10.1039/C0OB01033B

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