Peptides derived from two dynamically disordered proteins self-assemble into amyloid-like fibrils.

Short peptides derived from p14ARF and Hdm2 (14 and 15 amino acids in length, respectively), two cancer associated proteins, have been found to co-assemble into amyloid-like structures. Larger protein domains containing these peptide segments interact in cells and also undergo a disorder-to-order transition upon binding in vitro. In contrast to ...
the association of beta-strand assemblies with amyloid diseases, the system described herein utilizes the formation of binary, extended beta-strands as a novel mechanism of biomolecular assembly. The beta-strand-containing fibrils formed from these peptides may allow the directed assembly of decorated fibrils with applications as biological nanostructures.
Mesh Terms:
Amino Acid Sequence, Amyloid, Circular Dichroism, Microscopy, Electron, Molecular Sequence Data, Nuclear Proteins, Peptide Fragments, Protein Structure, Tertiary, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-mdm2, Spectroscopy, Fourier Transform Infrared, Tumor Suppressor Protein p14ARF
J. Am. Chem. Soc.
Date: Mar. 19, 2003
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