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      Ganglioside GM1 produces stable, short, and cytotoxic Aβ 40 protofibrils

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          Abstract

          Monosialoganglioside GM1-bound amyloid β-peptides have been found in patients’ brains exhibiting early pathological changes of Alzheimer's disease.

          Abstract

          Monosialoganglioside GM1-bound amyloid β-peptides have been found in patients’ brains exhibiting early pathological changes of Alzheimer's disease. Herein, we report the ability of non-micellar GM1 to modulate Aβ 40 aggregation resulting in the formation of stable, short, rod-like, and cytotoxic Aβ 40 protofibrils with the ability to potentiate both Aβ 40 and Aβ 42 aggregation.

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          Most cited references45

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          The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics.

          John Hardy, Dennis Selkoe (2002)
          It has been more than 10 years since it was first proposed that the neurodegeneration in Alzheimer's disease (AD) may be caused by deposition of amyloid beta-peptide (Abeta) in plaques in brain tissue. According to the amyloid hypothesis, accumulation of Abeta in the brain is the primary influence driving AD pathogenesis. The rest of the disease process, including formation of neurofibrillary tangles containing tau protein, is proposed to result from an imbalance between Abeta production and Abeta clearance.
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            Protein misfolding, functional amyloid, and human disease.

            Fabrizio Chiti, Christopher Dobson (2006)
            Peptides or proteins convert under some conditions from their soluble forms into highly ordered fibrillar aggregates. Such transitions can give rise to pathological conditions ranging from neurodegenerative disorders to systemic amyloidoses. In this review, we identify the diseases known to be associated with formation of fibrillar aggregates and the specific peptides and proteins involved in each case. We describe, in addition, that living organisms can take advantage of the inherent ability of proteins to form such structures to generate novel and diverse biological functions. We review recent advances toward the elucidation of the structures of amyloid fibrils and the mechanisms of their formation at a molecular level. Finally, we discuss the relative importance of the common main-chain and side-chain interactions in determining the propensities of proteins to aggregate and describe some of the evidence that the oligomeric fibril precursors are the primary origins of pathological behavior.
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              Molecular mechanism of Thioflavin-T binding to amyloid fibrils.

              Matthew Biancalana, Shohei Koide (2010)
              Intense efforts to detect, diagnose, and analyze the kinetic and structural properties of amyloid fibrils have generated a powerful toolkit of amyloid-specific molecular probes. Since its first description in 1959, the fluorescent dye Thioflavin-T (ThT) has become among the most widely used "gold standards" for selectively staining and identifying amyloid fibrils both in vivo and in vitro. The large enhancement of its fluorescence emission upon binding to fibrils makes ThT a particularly powerful and convenient tool. Despite its widespread use in clinical and basic science applications, the molecular mechanism for the ability of ThT to recognize diverse types of amyloid fibrils and for the dye's characteristic fluorescence has only begun to be elucidated. Here, we review recent progress in the understanding of ThT-fibril interactions at an atomic resolution. These studies have yielded important insights into amyloid structures and the processes of fibril formation, and they also offer guidance for designing the next generation of amyloid assembly diagnostics, inhibitors, and therapeutics. Copyright (c) 2010 Elsevier B.V. All rights reserved.
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                Author and article information

                Contributors
                Ayyalusamy Ramamoorthy: (View ORCID Profile)
                Journal
                Journal ID (publisher-id): CHCOFS
                Title: Chemical Communications
                Abbreviated Title: Chem. Commun.
                Publisher: Royal Society of Chemistry (RSC)
                ISSN (Print): 1359-7345
                ISSN (Electronic): 1364-548X
                Publication date Created: June 06 2023
                Publication date (Electronic): 2023
                Volume: 59
                Issue: 46
                Pages: 7040-7043
                Affiliations
                [1 ]Biophysics, Department of Chemistry, Biomedical Engineering, Macromolecular Science and Engineering, Michigan Neuroscience Institute, University of Michigan, Ann Arbor, MI 48109-1055, USA
                [2 ]Department of Neurology, University of Michigan, Ann Arbor, MI 48109, USA
                Article
                DOI: 10.1039/D3CC02186F
                SO-VID: 3b9d7967-ee4e-458b-aaca-de7645c47c93
                Copyright © © 2023
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                http://rsc.li/journals-terms-of-use

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