Glyceraldehyde-3-phosphate dehydrogenase tetramer dissociation and amyloid fibril formation induced by negatively charged membranes |
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Authors: | Leonardo M. Cortez |
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Affiliation: | Departamento Bioquímica de la Nutrición, Instituto Superior de Investigaciones Biológicas (CONICET-UNT), Chacabuco 461 (4000), Tucumán, Argentina Departamento Bioquímica de la Nutrición, Instituto de Química Biológica Dr. Bernabé Bloj, Chacabuco 461 (4000), Tucumán, Argentina |
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Abstract: | Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a multifunctional enzyme related with Huntington’s, Parkinson’s and Alzheimer’s diseases. The ability of negatively charged membranes to induce a rapid formation of GAPDH amyloid fibrils has been demonstrated, but the mechanisms by which GAPDH reaches the fibrillar state remains unclear. In this report, we describe the structural changes undergone by GAPDH at physiological pH and temperature conditions right from its interaction with acidic membranes until the amyloid fibril is formed. According to our results, the GAPDH-membrane binding induces a β-structuring process along with a loss of quaternary structure in the enzyme. In this way, experimental evidences on the initial steps of GAPDH amyloid fibrils formation pathway are provided. |
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Keywords: | Glyceraldehyde-3-phosphate dehydrogenase Infrared spectroscopy Protein-membrane interaction Amyloid |
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