ArticleInternational journal of biomedical nanoscience and nanotechnology2011
The impact of protein disulfide bonds on the amyloid fibril morphology.
Article in International journal of biomedical nanoscience and nanotechnology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- A Practical Guide to All-Atom and Coarse-Grained Molecular Dynamics Simulations Using Amber and Gromacs: A Case Study of Disulfide-Bond Impact on the Intrinsically Disordered Amyloid Beta.International journal of molecular sciences · 2024Article
- Non-Perturbative Identification and Subtyping of Amyloidosis in Human Kidney Tissue with Raman Spectroscopy and Machine Learning.Biosensors · 2023Article
- The Introduction of a Cysteine Residue Modulates The Mechanical Properties of Aromatic-Based Solid Aggregates and Self-Supporting Hydrogels.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- Molecular Spectroscopic Markers of Abnormal Protein Aggregation.Molecules (Basel, Switzerland) · 2020Review
- Reactivity of disulfide bonds is markedly affected by structure and environment: implications for protein modification and stability.Scientific reports · 2016Article
- Hydrogen sulfide inhibits amyloid formation.The journal of physical chemistry. B · 2015Article
- Is supramolecular filament chirality the underlying cause of major morphology differences in amyloid fibrils?Journal of the American Chemical Society · 2014Article
- Article
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Authors and funding
2 authors.
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Abstract
Amyloid fibrils are associated with many neurodegenerative diseases. Being formed from more than 20 different proteins that are functionally or structurally unrelated, amyloid fibrils share a common cross-β core structure. It is a well-accepted hypothesis that fibril biological activity and the associated toxicity vary with their morphology. Partial denaturation of a native protein usually precedes the initial stage of fibrillation, namely the nucleation process. Low pH and elevated temperature, typical conditions of amyloid fibril formation in vitro, resulted in partial denaturation of the proteins. Cleavage of disulfide bonds results typically in significant disruption of protein native structure and in the formation of the molten global state. Herein we report on a comparative investigation of fibril formation by apo-α-lactalbumin and its analog that contains only one of the four original disulfide bonds using deep UV resonance and non-resonance Raman spectroscopy and atomic force microscopy. Significant differences in the aggregation mechanism and the resulting fibril morphology were found.
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