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Fmoc-Diphenylalanine Self-Assembly Mechanism Induces Apparent pKa Shifts
Tang, C; Smith, A M; Collins, R F; Ulijn, R V; Saiani, A
Langmuir. 2009;25(16):9447.
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Abstract
We report the effect of pH on the self-assembly process of Fmoc-diphenylalanine (Fmoc-FF) into fibrils consisting of antiparallel β-sheets, and show that it results in two apparent pKa shifts of ∼6.4 and ∼2.2 pH units above the theoretical pKa (3.5). Using Fourier transform infrared (FTIR) spectroscopy, transmission electron microscopy (TEM), wide angle X-ray scattering (WAXS), and oscillatory rheology, these two transitions were shown to coincide with significant structural changes. An entangled network of flexible fibrils forming a weak hydrogel dominates at high pH, while nongelling flat rigid ribbons form at intermediate pH values. Overall, this study provides further understanding of the self-assembly mechanism of aromatic short peptide derivatives.
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