ArticleJournal of molecular biology2008
Aromatic cross-strand ladders control the structure and stability of beta-rich peptide self-assembly mimics.
Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Chemical Evolution of Early Macromolecules: From Prebiotic Oligopeptides to Self-Organizing Biosystems via Amyloid Formation.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Amyloidogenesis: What Do We Know So Far?International journal of molecular sciences · 2022Review
- Peptide-based supramolecular vaccine systems.Acta biomaterialia · 2021Review
- Tyrosine-Rich Peptides as a Platform for Assembly and Material Synthesis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2019Review
- Atomic model of a nonenveloped virus reveals pH sensors for a coordinated process of cell entry.Nature structural & molecular biology · 2016Article
- Aromatic cluster mutations produce focal modulations of β-sheet structure.Protein science : a publication of the Protein Society · 2015Article
- Influence of pH control in the formation of inclusion bodies during production of recombinant sphingomyelinase-D in Escherichia coli.Microbial cell factories · 2014Article
- Novel dimeric β-helical model of an ice nucleation protein with bridged active sites.BMC structural biology · 2011Article
- Molecular mechanism of Thioflavin-T binding to amyloid fibrils.Biochimica et biophysica acta · 2010Review
- Minimalist design of water-soluble cross-beta architecture.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Atomic-scale simulations confirm that soluble beta-sheet-rich peptide self-assemblies provide amyloid mimics presenting similar conformational properties.Biophysical journal · 2010Article
- Article
- Molecular mechanism of thioflavin-T binding to the surface of beta-rich peptide self-assemblies.Journal of molecular biology · 2009Article
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4 authors.
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Abstract
Though beta-rich self-assemblies comprise a major structural class of polypeptides, a detailed understanding of the determinants of their structure and stability is lacking. In particular, the roles of repetitive stretches of side chains running the long axis of these beta-sheets, termed "cross-strand ladders," remain poorly characterized due to the inherently insoluble and heterogeneous nature of self-assemblies. To overcome these experimental challenges, we have established a complementary experimental system termed "peptide self-assembly mimics" (PSAMs). The PSAMs capture a defined number of self-assembly-like peptide repeats within a soluble beta-rich protein, making structural and energetic studies possible. In this work, we investigated the role of cross-strand ladders containing aromatic residues, which are prominent in self-assembling peptides. A combination of solution data and high-resolution crystal structures revealed that a single cross-strand ladder consisting solely of Tyr significantly stabilized, rigidified, and flattened the PSAM beta-sheet. These characteristics would stabilize each beta-sheet layer of a self-assembly and direct sheet conformations compatible with lamination. Our results therefore provide a rationale for the abundance of aromatic amino acids in fibril-forming peptides and establish important roles of cross-strand Tyr ladders in the structure and stability of beta-rich peptide self-assemblies.
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