ArticleThe journal of physical chemistry. B2010
Simulation of two-dimensional ultraviolet spectroscopy of amyloid fibrils.
Article in The journal of physical chemistry. B, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed.
- Study of the γD-crystallin protein using two-dimensional infrared (2DIR) spectroscopy: experiment and simulation.The journal of physical chemistry. B · 2013Article
- Tracking the mechanism of fibril assembly by simulated two-dimensional ultraviolet spectroscopy.The journal of physical chemistry. A · 2013Article
- Distinguishing amyloid fibril structures in Alzheimer's disease (AD) by two-dimensional ultraviolet (2DUV) spectroscopy.Biochemistry · 2011Article
- Probing amyloid fibril growth by two-dimensional near-ultraviolet spectroscopy.The journal of physical chemistry. B · 2011Article
- Two-dimensional near-ultraviolet spectroscopy of aromatic residues in amyloid fibrils: a first principles study.Physical chemistry chemical physics : PCCP · 2011Article
- Two-dimensional ultraviolet (2DUV) spectroscopic tools for identifying fibrillation propensity of protein residue sequences.Angewandte Chemie (International ed. in English) · 2010Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Revealing the structure and aggregation mechanism of amyloid fibrils is essential for the treatment of over 20 diseases related to protein misfolding. Coherent two-dimensional (2D) infrared spectroscopy is a novel tool that provides a wealth of new insight into the structure and dynamics of biomolecular systems. Recently developed ultrafast laser sources are extending multidimensional spectroscopy into the ultraviolet (UV) region, and this opens up new opportunities for probing fibrils. In a simulation study, we show that 2DUV spectra of the backbone of a 32-residue β-amyloid (Aβ(9-40)) fibril associated with Alzheimer's disease and two intermediate prefibrillar structures carry characteristic signatures of fibril size and geometry that could be used to monitor its formation kinetics. The dependence of these signals on the fibril size and geometry is explored. We demonstrate that the dominant features of the β-amyloid fibril spectra are determined by intramolecular interactions within a single Aβ(9-40), and intermolecular interactions at the "external interface" have clear signatures in the fine details of these signals.
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Registered trials
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