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Literature DB >> 19173616

A new artificial beta-sheet that dimerizes through parallel beta-sheet interactions.

Abstract

This paper introduces a chemical model of a beta-sheet that dimerizes through parallel beta-sheet interactions in CDCl(3) solution. The model consists of two C-terminally linked dipeptides connected to a molecular template. (1)H NMR studies establish the beta-sheet folding and dimerization of the model system. This system corroborates that linking two peptide strands and blocking one edge of the assembly creates soluble, easy-to-study systems that participate in the types of interactions that occur widely in peptide and protein aggregates.

Entities: Chemical Disease Gene Species

Mesh：

Substances：
Proteins

Year: 2009 PMID： 19173616 PMCID： PMC2652689 DOI： 10.1021/ol802993v

Source DB: PubMed Journal: Org Lett ISSN： 1523-7052 Impact factor: 6.005

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References

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A new artificial beta-sheet that dimerizes through parallel beta-sheet interactions.

1. A structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMR.

2. 3D structure of Alzheimer's amyloid-beta(1-42) fibrils.

3. Structure of the cross-beta spine of amyloid-like fibrils.

4. What I have learned by using chemical model systems to study biomolecular structure and interactions.

5. The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy.

6. Tandem oligonucleotide synthesis on solid-phase supports for the production of multiple oligonucleotides.

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9. Relationship between nuclear magnetic resonance chemical shift and protein secondary structure.

10. Structural insights into the polymorphism of amyloid-like fibrils formed by region 20-29 of amylin revealed by solid-state NMR and X-ray fiber diffraction.