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Molecular and Cellular Biochemistry

, Volume 451, Issue 1–2, pp 165–171 | Cite as

Structural effects of methylglyoxal glycation, a study on the model protein MNEI

  • Serena LeoneEmail author
  • Jole Fonderico
  • Chiara Melchiorre
  • Andrea Carpentieri
  • Delia PiconeEmail author
Article

Abstract

The reaction of free amino groups in proteins with reactive carbonyl species, known as glycation, leads to the formation of mixtures of products, collectively referred to as advanced glycation endproducts (AGEs). These compounds have been implicated in several important diseases, but their role in pathogenesis and clinical symptoms’ development is still debated. Particularly, AGEs are often associated to the formation of amyloid deposits in conformational diseases, such as Alzheimer’s and Parkinson’s disease, and it has been suggested that they might influence the mechanisms and kinetics of protein aggregation. We here present the characterization of the products of glycation of the model protein MNEI with methylglyoxal and their effect on the protein structure. We demonstrate that, despite being an uncontrolled process, glycation occurs only at specific residues of the protein. Moreover, while not affecting the protein fold, it alters its shape and hydrodynamic properties and increases its tendency to fibrillar aggregation. Our study opens the way to in deep structural investigations to shed light on the complex link between protein post-translational modifications, structure, and stability.

Keywords

Protein glycation Advanced glycation endproducts Protein aggregation Protein hydrodynamics Post-translational modifications 

Notes

Funding

This work was supported by “Fondazione con il SUD,” Grant 2011-PDR-19.

Supplementary material

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Supplementary material 1 (PDF 32 KB)
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Supplementary material 2 (EPS 79 KB)
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Supplementary material 3 (EPS 136 KB)
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Supplementary material 4 (EPS 221 KB)

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Copyright information

© Springer Science+Business Media, LLC, part of Springer Nature 2018

Authors and Affiliations

  1. 1.Department of Chemical SciencesUniversity of Naples Federico II, Complesso Universitario di Monte Sant’AngeloNaplesItaly

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