Picture of mobile phone running fintech app

Fintech: Open Access research exploring new frontiers in financial technology

Strathprints makes available Open Access scholarly outputs by the Department of Accounting & Finance at Strathclyde. Particular research specialisms include financial risk management and investment strategies.

The Department also hosts the Centre for Financial Regulation and Innovation (CeFRI), demonstrating research expertise in fintech and capital markets. It also aims to provide a strategic link between academia, policy-makers, regulators and other financial industry participants.

Explore all Strathclyde Open Access research...

Effect of glycine substitution on fmoc-diphenylalanine self-assembly and gelation properties

Tang, C. and Ulijn, R. V. and Saiani, A. (2011) Effect of glycine substitution on fmoc-diphenylalanine self-assembly and gelation properties. Langmuir, 27 (23). pp. 14438-14449. ISSN 0743-7463

Full text not available in this repository. Request a copy from the Strathclyde author


We have investigated the self-assembly behavior of fluorenyl-9-methoxycarbonyl (Fmoc)-FG, Fmoc-GG, and Fmoc-GF and compared it to that of Fmoc-FF using potentiometry, fluorescence and infrared spectroscopy, transmission electron microscopy, wide-angle X-ray scattering, and oscillatory rheometry. Titration experiments revealed a substantially shifted apparent pK(a) transition for Fmoc-FG, Fmoc-GG, and Fmoc-GF. The apparent plc values observed correlated with the hydrophobicity (log P) of the Fmoc-dipeptide molecules. Fmoc-GG and Fmoc-GF were found to self-assemble only in their protonated form (below their apparent pK(a)), while Fmoc-FG formed self-assembled structures above and below its apparent pK(a). Fmoc-GG and Fmoc-FG were found to form hydrogels below their apparent pK(a) transitions in agreement with the entangled fibers morphologies revealed by TEM. Unlike Fmoc-FF and Fmoc-GG, Fmoc-FG showed unusual gelation behavior as gels were found to form upon heating. Fmoc-GF formed precipitates instead of a hydrogel below its apparent pK(a) in agreement with the formation of micrometer scale sheetlike structures observed by TEM. The fact that all four Fmoc-dipeptides were found to self-assemble suggests that the main driving force behind the self-assembly process is a combination of the hydrophobic and pi-pi interactions of the fluorenyl moieties with a secondary role for hydrogen bonding of the peptidic components. The nature of the peptidic tail was found to have a pronounced effect on the type of self-assembled structure formed. This work indicates that the substitution of phenylalanine by glycine significantly impacts on the mode of assembly and illustrates the versatility of aromatic peptide amphiphiles in the formation of structurally diverse nanostructures.