Mutant forms of Superoxide Dismutase 1(SOD1) have been linked to Familial Amyotrophic Lateral Sclerosis(fALS). Interestingly, this link has been shown to be independent of SOD1 catalytic activity as well as the observed presence of SOD1 rich aggregates in the spinal cords of patients with fALS. Current theories for disease development focus on the possible accumulation of a harmful SOD1 formation involving soluble oligomers. To study these oligomers, a method was developed to arrest transient SOD1 complexes by chemical crosslinking at various stages of aggregation. The results obtained establish the necessity for further augmentation of this methodology by both increasing the site-specificity of crosslinkers as well as biasing the system to preferentially form intramolecular crosslinks.

• This report represents the work of one or more WPI undergraduate students submitted to the faculty as evidence of completion of a degree requirement. WPI routinely publishes these reports on its website without editorial or peer review.

Creator

• Cohen, Noah Robert

Publisher

• Worcester Polytechnic Institute

Identifier

• E-project-042910-111712

Advisor

• Heilman, Destin

Year

• 2010

Sponsor

• UMass Medical School

Date created

• 2010-04-29

Resource type

• Major Qualifying Project

Major

• Biochemistry

Rights statement

• In Copyright