Preparation of diverse BODIPY diesters

The synthesis and properties of a variety of substituted BODIPY diesters is presented. We find that certain substitution patterns afford appreciable yields of the target compounds and that electronic effects result in predicable differential fluorescent behavior. Challenges to further water solubilize these dyes and/or provide new points of attachment for biological tagging remain, these strategies are discussed.     

Site-Specific Differences in Proteasome-Dependent Degradation of Monoubiquitinated α-Synuclein

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Semisynthetic, site-specific ubiquitin modification of α-synuclein reveals differential effects on aggregation

The process of neurodegeneration in Parkinson's Disease is intimately associated with the aggregation of the protein α-synuclein into toxic oligomers and fibrils. Interestingly, many of these protein aggregates are found to be post-translationally modified by ubiquitin at several different lysine residues. However, the inability to generate homogeneously ubiquitin modified α-synuclein at each site has prevented the understanding of the specific biochemical consequences. We have used protein semisynthesis to generate nine site-specifically ubiquitin modified α-synuclein derivatives and have demonstrated that different ubiquitination sites have differential effects on α-synuclein aggregation.