Forced amyloidogenic cooperativity of structurally incompatible peptide segments: Fibrillization behavior of highly aggregation-prone A-chain fragment of insulin coupled to all-L, and alternating L/D octaglutamates
Abstract:Self-aggregation of individual polypeptide chains into amyloid fibrils is driven by interactions between amyloidogenic segments of whole proteins. The interplay between aggregation-prone and aggregation-resistant fragments within a single polypeptide chain is not well understood. Here, we examine fibrillization behavior of two designed chimeric peptides, ACC1-13E8 and ACC1-13E8(L/D), in which the highly amyloidogenic fragment of insulin’s A-chain (ACC1-13) is extended by an octaglutamate segment composed of al… Show more
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