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Aggregation and the Intrinsic Structural Disorder of Dipeptide Repeat Peptides of C9orf72-Related Amyotrophic Lateral Sclerosis and Frontotemporal Dementia Characterized by NMR

J Phys Chem B. 2021-11; 
Bankala Krishnarjuna, Magdalena I Ivanova, Ayyalusamy Ramamoorthy
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Proteins, Expression, Isolation and Analysis … The dipeptide hexa-repeats; (GP) 6 , (GR) 6 , and (GA) 6 were purchased from GenScript with a purity of 98.5%, 98.9%, and 98.1%, respectively, and used without further purification. D 2 O used in NMR samples for deuterium locking was purchased from Cambridge Isotope … Get A Quote

摘要

Dipeptide repeats (DPRs) are known to play important roles in C9ORF72-related amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD). Studies on DPRs have reported on the kinetics of aggregation, toxicity, and low-resolution morphology of the aggregates of these peptides. While the dipeptide hexa-repeats of Gly-Pro [(GP)] have been shown to be nonaggregating, Gly-Ala [(GA)] and Gly-Arg [(GR)] exhibited the formation of neurotoxic aggregates. However, structural studies of these DPRs have been elusive. In this study, we explored the feasibility of a high-resolution monitoring of a real-time aggregation of these peptides in a solution by using NMR experiments. Although (GP) is disordered and nonagg... More

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