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. 2009 Aug 10;10(8):2319-27.
doi: 10.1021/bm9005084.

Self-assembled hydrogels from poly[N-(2-hydroxypropyl)methacrylamide] grafted with beta-sheet peptides

Larisa C Radu-Wu  1 , Jiyuan Yang, Kuangshi Wu, Jindrich Kopecek
Affiliations

Self-assembled hydrogels from poly[N-(2-hydroxypropyl)methacrylamide] grafted with beta-sheet peptides

Larisa C Radu-Wu et al. Biomacromolecules. .

Abstract

A new hybrid hydrogel based on poly[N-(2-hydroxypropyl)methacrylamide] grafted with a beta-sheet peptide, Beta11, was designed. Circular dichroism spectroscopy indicated that the folding ability of beta-sheet peptide was retained in the hybrid system, whereas the sensitivity of the peptide toward temperature and pH variations was hindered. The polymer backbone also prevented the twisting of the fibrils that resulted from the antiparallel arrangement of the beta-strands, as proved by Fourier transform infrared spectroscopy. Thioflavin T binding experiments and transmission electron microscopy showed fibril formation with minimal lateral aggregation. As a consequence, the graft copolymer self-assembled into a hydrogel in aqueous environment. This process was mediated by association of beta-sheet domains. Scanning electron microscopy revealed a particular morphology of the network characterized by long-range order and uniformly aligned lamellae. Microrheology results confirmed that concentration-dependent gelation occurred.

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Figures

Figure 1
Figure 1
Synthesis of poly(HPMA)-g-CGGBeta11 graft copolymer and its self-assembly into a hydrogel via association of pendant β-sheet peptide strands.
Figure 2
Figure 2
A. Temperature-dependent CD spectra of Beta11 peptide (the arrow indicates the change of spectrum upon temperature increase); B. Temperature-dependent CD spectra of poly(HPMA)-g-CGGBeta11 graft copolymer; C. Temperature effect on the secondary structure of Beta11 and poly(HPMA)-g-CGGBeta11, recorded as change in ellipticity at 218 nm; D. pH-Dependent CD spectra of Beta11 peptide; E. pH-Dependent CD spectra of poly(HPMA)-g-CGGBeta11 graft copolymer.
Figure 3
Figure 3
FTIR spectra (solid) and second-derivatives (dotted) of A. Beta11 peptide; B. poly(HPMA)-g-CGGBeta11 graft copolymer.
Figure 4
Figure 4
A. Fluorescence emission spectra (λexc = 440 nm) of Beta11 peptide and poly(HPMA)-g-CGGBeta11 graft copolymer after addition of 50 µM ThT. ThT alone was used as blank; B. CR binding assay; C. Differential spectra of (Beta11/CR)-CR and (poly(HPMA)-g-CGGBeta11/CR)-CR showing the points of maximum absorption.
Figure 5
Figure 5
A. TEM image of negatively stained Beta11 fibrils; B. TEM image of negatively stained poly(HPMA)-g-CGGBeta11 fibrils; C. SEM image of freeze-dried 0.4 wt % Beta11 gel; D. SEM image of freeze-dried 0.4 wt % poly(HPMA)-g-CGGBeta11 gel (the inset is the image of the cross-sectioned copolymer gel).
Figure 6
Figure 6
Mean square displacement (MSD) as a function of lag time for 0.52 µm amidine-modified PS particles in water solutions/gels at different concentrations of A. Beta11 peptide; B. poly(HPMA)-g-CGGBeta11 graft copolymer.
Figure 7
Figure 7
Frequency-dependent linear viscoelastic moduli for 0.52 µm amidine-modified PS particles in water solutions/gels of A. Beta11 peptide (solid symbols for loss modulus, G”, and half-open red symbols for storage modulus, G’); B. poly(HPMA)-g-CGGBeta11 graft copolymer (open symbols for loss modulus, G”, and half-solid red symbols for storage modulus, G’).
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