Hierarchical approach for the rational construction of helix-containing nanofibrils using α, β-peptides. Issue 7 (20th January 2021)

• Record Type: Journal Article
• Authors: Szefczyk, Monika; Szulc, Natalia; Gąsior-Głogowska, Marlena; Modrak-Wójcik, Anna; Bzowska, Agnieszka; Majstrzyk, Wojciech; Taube, Michał; Kozak, Maciej; Gotszalk, Teodor; Rudzińska-Szostak, Ewa; Berlicki, Łukasz
• Is Part Of: Nanoscale. Volume 13:Issue 7(2021)
• Page Start: 4000
• Page End: 4015
• Publication Date: 2021-01-20
• Subjects: Nanoscience -- Periodicals; Nanotechnology -- Periodicals; 620.505
• DOI: 10.1039/d0nr04313c
• Languages: English
• ISSNs: 2040-3364

Abstract

Abstract : The incorporation of cyclopentane-based beta-amino acid in the sequence of peptide forming coiled-coil induced formation of nanofibrils. Abstract : The rational design of novel self-assembled nanomaterials based on peptides remains a great challenge in modern chemistry. A hierarchical approach for the construction of nanofibrils based on α, β-peptide foldamers is proposed. The incorporation of a helix-promoting trans -(1 S, 2 S )-2-aminocyclopentanecarboxylic acid residue in the outer positions of the model coiled-coil peptide led to its increased conformational stability, which was established consistently by the results of CD, NMR and FT-IR spectroscopy. The designed oligomerization state in the solution of the studied peptides was confirmed using analytical ultracentrifugation. Moreover, the cyclopentane side chain allowed additional interactions between coiled-coil-like structures to direct the self-assembly process towards the formation of well-defined nanofibrils, as observed using AFM and TEM techniques.