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Investigating the Formation of a Repulsive Hydrogel of a Cationic 16mer Peptide at Low Ionic Strength in Water by Vibrational Spectroscopy and Rheology

Abstract

The cationic peptide (AAKA)4 (AK16) exhibits a high propensity for aggregation into β-sheet-like structures in spite of the high positive charge of its protonated lysine side chains. Upon incubation into an aqueous solution, the peptide maintains a metastable β-sheet-like structure with fibrillar content, the apparent stability of which increases with peptide concentration. In the presence of a sufficiently high concentration of anions, the peptide spontaneously forms a hydrogel at millimolar concentrations. Interestingly, we find that even in the absence of gel-supporting anions, the peptide is capable of forming a hydrogel in the centimolar range. Rheological data reveal that the gel is a stable elastic solid. These data show that the peptide can overcome the repulsive interactions between the positively charged ammonium groups of the lysine residues. The addition of 1 M NaCl just accelerates this process. Atomic force microscopy images of the peptide gel reveal fibrils with thicknesses between 4 and 8 nm, which suggests that they contain multiple layers of sheets. We propose that long tapes of β-sheet are arranged in fibrils via stacking of alternating interfaces induced by hydrophobic interactions between alanine side chains and by the formation of a hydrogen bonded water network between hydrophilic sides of AK16 β-sheets, which leads to the observed immobilization of the solvent in the formed hydrogel. Water immobilization is proposed as the likely cause for a significant increase in the amide I′ oscillator strength of the formed β-sheet structures.

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Authors

DiGuiseppi, David; Kraus, Jodi; Toal, Siobhan E.; Alvarez, Nicolas; Schweitzer-Stenner, Reinhard

Citation

D. Diguiseppi, J. Kraus, S. E. Toal, N. J. Alvarez, and R. Schweitzer-Stenner, ‘Investigating the formation of a repulsive hydrogel of a cationic 16mer peptide at low ionic strength in water by vibrational spectroscopy and rheology’, Journal of Physical Chemistry B, vol. 120, no. 38, pp. 10079–10090, Sep. 2016, DOI: 10.1021/acs.jpcb.6b07673