Comparison of the self‐assembly and cytocompatibility of conjugates of Fmoc (9‐fluorenylmethoxycarbonyl) with hydrophobic, aromatic, or charged amino acids

Castelletto, V., de Mello, L., da Silva, E. R. ORCID: https://orcid.org/0000-0001-5876-2276, Seitsonen, J. and Hamley, I. W. ORCID: https://orcid.org/0000-0002-4549-0926 (2024) Comparison of the self‐assembly and cytocompatibility of conjugates of Fmoc (9‐fluorenylmethoxycarbonyl) with hydrophobic, aromatic, or charged amino acids. Journal of Peptide Science. ISSN 1099-1387 doi: 10.1002/psc.3571

Abstract/Summary

The self-assembly in aqueous solution of three Fmoc-amino acids with hydrophobic (aliphatic or aromatic, alanine or phenylalanine) or hydrophilic cationic residues (arginine) is compared. The critical aggregation concentrations were obtained using intrinsic fluorescence or fluorescence probe measurements, and conformation was probed using circular dichroism spectroscopy. Self-assembled nanostructures were imaged using cryo-transmission electron microscopy and small-angle X-ray scattering (SAXS). Fmoc-Ala is found to form remarkable structures comprising extended fibril-like objects nucleating from spherical cores. In contrast, Fmoc-Arg self-assembles into plate-like crystals. Fmoc-Phe forms extended structures, in a mixture of straight and twisted fibrils coexisting with nanotapes. Spontaneous flow alignment of solutions of Fmoc-Phe assemblies is observed by SAXS. The cytocompatibility of the three Fmoc-amino acids was also compared via MTT [3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide] mitochondrial activity assays. All three Fmoc-amino acids are cytocompatible with L929 fibroblasts at low concentration, and Fmoc-Arg shows cell viability up to comparatively high concentration (0.63 mM).

Item Type	Article
URI	https://reading-clone.eprints-hosting.org/id/eprint/115291
Item Type	Article
Refereed	Yes
Divisions	Interdisciplinary centres and themes > Chemical Analysis Facility (CAF) Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
Publisher	European Peptide Society and John Wiley & Sons
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