A 13-residue peptide, referred to as the KD peptide, has previously been shown to form a hydrogel under physiological conditions by means of a cross-linked network consisting of extended β-sheet fibrils. This project investigates uncapped variants of this peptide and a series of truncated sequences, with the aim of finding an optimal hydrogel-forming core. The peptides were made using solid phase methodology and purified by HPLC. Hydrogelation properties were then assessed using visual inspection, rheology, and cryo-TEM. It was found that Sequence 6 (S6) and Sequence 4 (S4), variants with 6 and 4 residues removed from the N-terminus, respectively, formed a hydrogel that underwent phase separation. Uncapped versions of KD (C-uncapped, N-uncapped, and both ends uncapped) formed a gel only at relatively high concentrations. Future directions of this project include the synthesis, purification, and hydrogelation studies of S5, as well as IR spectroscopy of the uncapped versions of the KD peptide and potentially other truncated sequences in order to identify the sequence with the most favorable hydrogelation properties.

Effects of endcapping and truncation of a hydrogel-forming peptide on its structural and materials properties

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

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