Composition and Conformation of Hetero‐ versus Homo‐Fluorinated Triazolamers Influence their Activity on Islet Amyloid Polypeptide Aggregation

• Published in: Chemistry : a European journal Vol. 30; no. 28; pp. e202303887 - n/a
• Main Authors: Laxio Arenas, José, Lesma, Jacopo, Ha‐Duong, Tap, Ranjan Sahoo, Bikash, Ramamoorthy, Ayyalusamy, Tonali, Nicolo, Soulier, Jean‐Louis, Halgand, Frédéric, Giraud, François, Crousse, Benoît, Kaffy, Julia, Ongeri, Sandrine
• Format: Journal Article
• Language: English
• Published: Weinheim Wiley Subscription Services, Inc 17.05.2024; Wiley-VCH Verlag
• Subjects: Aggregation; Amino acids; Amylin; amyloid; beta-hairpin; Chemical Sciences; Fluorescence; Fluorescence spectroscopy; Fluorination; Fluorine; foldamer; Labeling; Mass spectrometry; Mass spectroscopy; Medicinal Chemistry; Molecular dynamics; NMR; Nuclear magnetic resonance; Nucleotide sequence; peptidomimetic; Polypeptides; Proteins; triazole

Novel fluorinated foldamers based on aminomethyl‐1,4‐triazolyl‐difluoroacetic acid (1,4‐Tz−CF2) units were synthesized and their conformational behaviour was studied by NMR and molecular dynamics. Their activity on the aggregation of the human islet amyloid polypeptide (hIAPP) amyloid protein was ev...