Oxidation Enhances Human Serum Albumin Thermal Stability and Changes the Routes of Amyloid Fibril Formation
| Autor: | Gianluca Di Cara, Vito Foderà, Maurizio Leone, Valeria Vetri, Giuseppe Sancataldo, Valeria Militello |
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| Přispěvatelé: | Sancataldo, G, Vetri, V, Foderà, V, Di Cara, G, Militello, V, Leone, M |
| Jazyk: | angličtina |
| Rok vydání: | 2014 |
| Předmět: |
Macromolecular Assemblies
Protein Folding lcsh:Medicine Protein aggregation Biochemistry Physical Chemistry 01 natural sciences Protein Structure Secondary Protein structure Pathology lcsh:Science chemistry.chemical_classification 0303 health sciences Multidisciplinary biology Protein Stability Chemistry Physics Neurodegeneration Temperature Neurodegenerative Diseases Human serum albumin Neurology Medicine Oxidation-Reduction Molecular Pathology Research Article medicine.drug Amyloid Biophysics Serum albumin Protein degradation 010402 general chemistry 03 medical and health sciences Diagnostic Medicine medicine Humans Protein Interactions Biology Serum Albumin 030304 developmental biology Amyloid Fluorescence Oxidation Protein aggregation Spectoscopy Light Scattering Serum Albumin Reactive oxygen species lcsh:R Proteins Hydrogen Peroxide medicine.disease Protein tertiary structure 0104 chemical sciences Kinetics biology.protein lcsh:Q Protein Multimerization General Pathology |
| Zdroj: | PLoS ONE, Vol 9, Iss 1, p e84552 (2014) PLoS ONE PloS one 9 (2014). doi:10.1371/journal.pone.0084552 info:cnr-pdr/source/autori:Sancataldo, Giuseppe; Vetri, Valeria; Fodera, Vito; Di Cara, Gianluca; Militello, Valeria; Leone, Maurizio/titolo:Oxidation Enhances Human Serum Albumin Thermal Stability and Changes the Routes of Amyloid Fibril Formation/doi:10.1371%2Fjournal.pone.0084552/rivista:PloS one/anno:2014/pagina_da:/pagina_a:/intervallo_pagine:/volume:9 |
| Popis: | Oxidative damages are linked to several aging-related diseases and are among the chemical pathways determining protein degradation. Specifically, interplay of oxidative stress and protein aggregation is recognized to have a link to the loss of cellular function in pathologies like Alzheimer's and Parkinson's diseases. Interaction between protein and reactive oxygen species may indeed induce small changes in protein structure and lead to the inhibition/modification of protein aggregation process, potentially determining the formation of species with different inherent toxicity. Understanding the temperate relationship between these events can be of utmost importance in unraveling the molecular basis of neurodegeneration. In this work, we investigated the effect of hydrogen peroxide oxidation on Human Serum Albumin (HSA) structure, thermal stability and aggregation properties. In the selected conditions, HSA forms fibrillar aggregates, while the oxidized protein undergoes aggregation via new routes involving, in different extents, specific domains of the molecule. Minute variations due to oxidation of single residues affect HSA tertiary structure leading to protein compaction, increased thermal stability, and reduced association propensity. |
| Databáze: | OpenAIRE |
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