Abstract
β-Sheet forming peptides have attracted significant interest for the design of hydrogels for biomedical applications. One of the main challenges is the control and understanding of the correlations between peptide molecular structure, the morphology, and topology of the fiber and network formed as well as the macroscopic properties of the hydrogel obtained. In this work, we have investigated the effect that functionalizing these peptides through their hydrophobic face has on their self-assembly and gelation. Our results show that the modification of the hydrophobic face results in a partial loss of the extended β-sheet conformation of the peptide and a significant change in fiber morphology from straight to kinked. As a consequence, the ability of these fibers to associate along their length and form large bundles is reduced. These structural changes (fiber structure and network topology) significantly affect the mechanical properties of the hydrogels (shear modulus and elasticity).
Highlights
The use of noncovalent molecular self-assembly to construct materials has become a prominent strategy offering practical routes for the construction of increasingly functional materials
The exploitation of peptides and their self-assembling properties to design hydrogels in particular has been the focus of significant efforts due to their potential for use in a variety of biomedical applications such as cell therapy,[1,2] tissue regeneration,[3−8] and drug delivery.[9−11] A number of molecular designs have been developed for the synthesis of selfassembling peptides with the four main families being amphiphilic peptides,[12] short peptide derivatives, α-helix/ coiled-coil peptides,[13,14] and β-sheet peptides.[15−17] All these designs allow the synthesis of peptides that under appropriate conditions self-assemble to form elongated fibers
We have investigated the effect of functionalizing the β-sheet forming peptide FEFKFEFKK through the hydrophobic face by replacing one of the phenyl ring groups with a bromomaleimide group
Summary
The use of noncovalent molecular self-assembly to construct materials has become a prominent strategy offering practical routes for the construction of increasingly functional materials. We have recently investigated the self-assembly and gelation properties of a family of β-sheet peptides[18−20] based on the design developed by Zhang and co-workers.[21−23]. This design, which is based on the alternation of hydrophilic and hydrophobic residues, allows the synthesis of peptides that self-assemble into antiparallel β-sheet fibrils. It is thought that in order to minimize contact between water and the hydrophobic faces, these β-sheet fibrils associate by pairing to form β-sheet fibers with the hydrophobic residue side chains buried in the fiber core (Figure 1)
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