Peptides Derived from Two Dynamically Disordered Proteins Self-Assemble into Amyloid-like Fibrils
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- 作者：Brian Bothner ; Yves Aubin ; and Richard W. Kriwacki
- 刊名：Journal of the American Chemical Society
- 出版年：2003
- 出版时间：March 19, 2003
- 年：2003
- 卷：125
- 期：11
- 页码：3200 - 3201
- 全文大小：81K
- 年卷期：v.125,no.11(March 19, 2003)
- ISSN：1520-5126
文摘
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 
-strand assemblies with amyloid diseases, the system described herein utilizes the formation of binary, extended -strands as a novel mechanism of biomolecular assembly. The -strand-containing fibrils formed from these peptides may allow the directed assembly of decorated fibrils with applications as biological nanostructures.
-strand assemblies with amyloid diseases, the system described herein utilizes the formation of binary, extended -strands as a novel mechanism of biomolecular assembly. The -strand-containing fibrils formed from these peptides may allow the directed assembly of decorated fibrils with applications as biological nanostructures.