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Its medicinal-chemistry program, described in detail by Kruse and colleagues, introduced several deliberate substitutions into the amylin backbone: residues borrowed from rat amylin (which does not readily form fibrils) to blunt the aggregation tendency, an engineered salt bridge to stabilize the central helix, and a C 20 fatty-diacid moiety attached through a linker to promote reversible binding to serum albumin

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Combined, these mechanisms help reduce extended inflammatory damage