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The medicinal-chemistry programme that produced cagrilintide, described by Kruse and colleagues in the Journal of Medicinal Chemistry in 2021, addressed this by re-engineering the amylin backbone with structural elements borrowed from calcitonin (a related, non-aggregating peptide) and attaching a fatty-acid side chain that enables reversible binding to serum albumin [1]

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Takie cige, niepulsacyjne dziaanie odbiega od naturalnego, epizodycznego wzorca wydzielania hormonu wzrostu i teoretycznie zwiksza ryzyko efektw zwizanych z nadmiarem GH, opisanych w poprzedniej sekcji

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