Abstract

The aggregation of proteins to form amyloids is implicated in several diseases such as Alzheimer’s Disease, Parkinson’s Disease, and many others. This aggregation has several stages, progressing from isolated protein molecules (monomers) to small aggregates (oligomers), which are toxic to cells, and finally to large, string-like mature aggregates. Despite this association with disease, functional amyloids, which have normal biological functions, also result from protein aggregation. Kassinin, an amphibian peptide involved in nerve signal transmission, is a model system for functional amyloid study. To compare the aggregation of functional and disease-causing amyloids, we previously synthesized a fluorine-labeled kassinin through solid-phase peptide synthesis, purified the peptide by HPLC, and monitored the aggregation by 19F NMR in the presence of various additive molecules. One of the additives the seemed to produce significant results was the sugar derivative mannitol, which directed our synthesis of a glycosylated version of F-kassinin. Although 19F NMR data with mannitol was unable to be replicated, the successful synthesis of glycosylated F-kassinin was evidenced by MS data. Examining the aggregation process of functional amyloids and contrasting with published data on disease-associated amyloids will contribute to a clearer understanding of the disease process of protein aggregation associated diseases.