Ala97Ser(A97S)為台灣家族性類澱粉多發性神經病變(familial amyloid polyneuropathy, FAP)病人的主要轉運蛋白(transthyretin, TTR)變異型而有別世界上常見的Val30Met，小分子藥物tafamidis可以穩定四合體變異轉運蛋白，減少單元體的形成，進而減少類澱粉蛋白的沉積，達到延緩病情的效果。然而對於台灣主要變異型A97S的生物特徵及tafamidis對其藥理效應的了解仍然有限。台大貴重儀器中心特高場核磁共振儀服務協助中研院原分所余慈顏團隊了解A97S-TTR與tafamidis在甲狀腺素結合袋(thyroxine binding pocket)的結合位點(binding site)，進而證實tafamidis對A97S-TTR的結構調節效應，顯示tafamidis對A97S-TTR的台灣主要FAP病人的治療潛力。此研究成果發表於Ann. Clin. Transl. Neurol.。

(A) Mapping of significantly perturbed residues in red color on the ribbon representation of the WT TTR using
crystal structure, where the thyroxine binding sites are indicated with black box; (B) mapping of significantly perturbed residues on the ribbon representation of the dimer-dimer interface of the WT TTR using crystal structure; (C) mapping of significantly perturbed residues on the ribbon representation of the dimer-dimer interface of A97S TTR using a homology model generated based on the WT-TTR crystal structure