Oxidation Enhances Human Serum Albumin Thermal Stability and Changes the Routes of Amyloid Fibril Formation

Maurizio Leone, Valeria Vetri, Giuseppe Sancataldo, Valeria Militello, Vito Foderà, Gianluca Di Cara, Gianluca Di Cara, Valeria Vetri, Valeria Militello, Maurizio Leone, Gianluca Di Cara

Risultato della ricerca: Articlepeer review

44 Citazioni (Scopus)

Abstract

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.
Lingua originaleEnglish
Numero di pagine11
RivistaPLoS One
Volume9(1)
Stato di pubblicazionePublished - 2014

All Science Journal Classification (ASJC) codes

  • ???subjectarea.asjc.1300.1300???
  • ???subjectarea.asjc.1100.1100???
  • General

Fingerprint Entra nei temi di ricerca di 'Oxidation Enhances Human Serum Albumin Thermal Stability and Changes the Routes of Amyloid Fibril Formation'. Insieme formano una fingerprint unica.

Cita questo