ArticleProtein science : a publication of the Protein Society2007
The first step of hen egg white lysozyme fibrillation, irreversible partial unfolding, is a two-state transition.
Article in Protein science : a publication of the Protein Society, 2007. 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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13 citing papers in PubMed, 69 citations in OpenAlex.
- Spontaneous aging of mature amyloids alters structural stability, cytotoxicity, and susceptibility to biological clearance.Cell death discovery · 2026Article
- Sound-mediated nucleation and growth of amyloid fibrils.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Nanoscale structural characterization of transthyretin aggregates formed at different time points of protein aggregation using atomic force microscopy-infrared spectroscopy.Protein science : a publication of the Protein Society · 2023Article
- Protein-to-lipid ratio uniquely changes the rate of lysozyme aggregation but does not significantly alter toxicity of mature protein aggregates.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2023Article
- Analysis of the enzymatic degradation of lysozyme fibrils using a combination method of non-denaturing gel electrophoresis and double staining with Coomassie Brilliant Blue G-250 and R-250 dyes.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2023Article
- Lipids uniquely alter secondary structure and toxicity of lysozyme aggregates.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2022Article
- Identification of Novel 1,3,5-Triphenylbenzene Derivative Compounds as Inhibitors of Hen Lysozyme Amyloid Fibril Formation.International journal of molecular sciences · 2019Article
- Ultraviolet Resonance Raman Spectroscopic Markers for Protein Structure and Dynamics.Trends in analytical chemistry : TRAC · 2018Article
- Analysis of core region from egg white lysozyme forming amyloid fibrils.International journal of biological sciences · 2013Article
- UV resonance Raman investigations of peptide and protein structure and dynamics.Chemical reviews · 2012Review
- Article
- The impact of protein disulfide bonds on the amyloid fibril morphology.International journal of biomedical nanoscience and nanotechnology · 2011Article
- Discriminant analysis of Raman spectra for body fluid identification for forensic purposes.Sensors (Basel, Switzerland) · 2010Article
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Authors and funding
6 authors at 2 institutions in 1 country.
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Abstract
Amyloid fibril depositions are associated with many neurodegenerative diseases as well as amyloidosis. The detailed molecular mechanism of fibrillation is still far from complete understanding. In our previous study of in vitro fibrillation of hen egg white lysozyme, an irreversible partially unfolded intermediate was characterized. A similarity of unfolding kinetics found for the secondary and tertiary structure of lysozyme using deep UV resonance Raman (DUVRR) and tryptophan fluorescence spectroscopy leads to a hypothesis that the unfolding might be a two-state transition. In this study, chemometric analysis, including abstract factor analysis (AFA), target factor analysis (TFA), evolving factor analysis (EFA), multivariate curve resolution-alternating least squares (ALS), and genetic algorithm, was employed to verify that only two principal components contribute to the DUVRR and fluorescence spectra of soluble fraction of lysozyme during the fibrillation process. However, a definite conclusion on the number of conformers cannot be made based solely on the above spectroscopic data although chemometric analysis suggested the existence of two principal components. Therefore, electrospray ionization mass spectrometry (ESI-MS) was also utilized to address the hypothesis. The protein ion charge state distribution (CSD) envelopes of the incubated lysozyme were well fitted with two principal components. Based on the above analysis, the partial unfolding of lysozyme during in vitro fibrillation was characterized quantitatively and proven to be a two-state transition. The combination of ESI-MS and Raman and fluorescence spectroscopies with advanced statistical analysis was demonstrated to be a powerful methodology for studying protein structural transformations.
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