Faculty Advisor

Heilman, Destin

Abstract

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.

Publisher

Worcester Polytechnic Institute

Date Accepted

April 2010

Major

Biochemistry

Project Type

Major Qualifying Project

Accessibility

Unrestricted

Advisor Department

Chemistry and Biochemistry

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