Published January 28, 2019 | Version v1
Dataset Open

A time-course analysis using Differential Static Light Scattering (DSLS) of purified HTT1-3144 Q23 - 2019/01/28

Authors/Creators

  • 1. Structural Genomics Consortium, University of Toronto
  • 2. CHDI Foundation

Description

Project: Biophysical investigation of purified HTT protein samples

Experiment: A time-course analysis using Differential Static Light Scattering (DSLS) of purified HTT1-3144Q23 

Date completed:­ 2019/01/28

Rationale: Time and resources in the HD field have been primarily focussed on understanding HTT aggregation looking as caspase cleavage products spanning aa. 1-586 or exon 1 spanning aa. 1-90. However, we know that HTT protein purified in its apo form is able to self-associate into larger oligomeric species and that monomer, dimer and larger species are found following FLAG-affinity chromatography as determined by size-exclusion chromatography (SEC) and SEC-multi-angle light scattering (SEC-MALS). This experiment aimed to begin to investigate how HTT self-associates and aggregates over time in a range of different conditions. 

Notes

Dr. Harding is the recipient of the Huntington's Disease Society of America Berman Topper Career Development Fellowship which funds and supports this research, in addition to generous funding from the CHDI Foundation and the Huntington Society of Canada. The SGC is a registered charity (number 1097737) that receives funds from AbbVie, Bayer Pharma AG, Boehringer Ingelheim, Canada Foundation for Innovation, Eshelman Institute for Innovation, Genome Canada through Ontario Genomics Institute [OGI-055], Innovative Medicines Initiative (EU/EFPIA) [ULTRA-DD grant no. 115766], Janssen, Merck KGaA, Darmstadt, Germany, MSD, Novartis Pharma AG, Ontario Ministry of Research, Innovation and Science (MRIS), Pfizer, São Paulo Research Foundation-FAPESP, Takeda, and Wellcome.

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