2017/12/14 by Mary Rose Hilaire, Bei Ding, Debopreeti Mukherjee +2 · 2 citations
Materials Science · Biochemistry, Genetics and Molecular Biology · #Supramolecular Self-Assembly in Materials #Protein Structure and Dynamics #Chemical Synthesis and Analysis
paper · doi:10.1021/jacs.7b09262
openalex publication_date 2017/12/14 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/01
Herein, we combine several methods to characterize the fibrils formed by a TTR 105–115 mutant in which Leu111 is replaced by the unnatural amino acid aspartic acid 4-methyl ester. We find that this mutant peptide exhibits significantly different aggregation behavior than the wild-type peptide: (1) it forms fibrils with a much faster rate, (2) its fibrils lack the long-range helical twists observed in TTR 105–115 fibrils, (3) its fibrils exhibit a giant far-UV circular dichroism signal, and (4) its fibrils give rise to an unusual amide I′ band consisting of four distinct and sharp peaks. On the basis of these results and also several previous computational studies, we hypothesize that the fibrils formed by this TTR mutant peptide contain both β- and α-sheets.