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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]

doi:10.1038/178064a0

Ma S, He L-L, Zhang G-R, Zuo Q-J, Wang Z-L, Zhai J-L, et al

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