Peptides derived from two dynamically disordered proteins self-assemble into amyloid-like fibrils |
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Authors: | Bothner Brian Aubin Yves Kriwacki Richard W |
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Affiliation: | Department of Structural Biology, St. Jude Children's Research Hospital, Memphis, Tennessee 38105, USA. |
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Abstract: | 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. |
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