The spontaneous deamidation of asparagine to aspartate in Cu, Zn superoxide dismutase (SOD1) has been historically overlooked as a possible mechanism by which the wild-type SOD1 protein can be converted to an isoform that mimics mutant forms of SOD1 that cause amyotrophic lateral sclerosis (ALS). Nevertheless, the deamidation of Asn to Asp is chemically equivalent to Asn:Asp missense mutations to SOD1 that cause ALS (e.g., N86D and N139D). In this project, we determine how the deamidation of different asparagine to aspartate affects the structure, thermostability and rate of fibrillization of SOD1. We also present mass spectrometric data showing the presence of Asn deamidation in SOD1 in vivo.

Deamidation of asparagine in Cu, Zn superoxide dismutase

248th National Meeting (2014)

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