Abstract
A short 7-residue stretch from β-amyloid, Aβ16–22 (Ac-KLVFFAE-am), yields typical amyloid-like fibrils at neutral pH. The Phe–Phe cassette present in the peptide is believed to be critical for its self-assembly. We report that the aromatic analogue Aβ16–22(F20Y) forms self-supporting soft gels at concentrations ≥2 mM even though the end-capped parent peptide does not form hydrogel up to 20 mM (1.8% w/w) concentration. The hydrogel is made up of distinct amyloid-like fibers. The storage modulus of 20 mM gel is ∼3–5-fold higher than the loss modulus in the 2–3000 rad/s angular frequency range, indicating distinct elastic properties. The hydrogel supports the growth of rat pancreatic cells (RIN-5F), human embryonic kidney cells (HEK-293), baby hamster kidney cells (BHK-21), and human neuroblastoma cells (IMR-32). The cells grow in clusters as is anticipated in a three-dimensional matrix. The rat pancreatic cells produced insulin, suggesting that they are functional inside the gel.
Highlights
Gels play an important role in our day-to-day life; toothpaste gels, shaving gels, and shampoos are some of the examples. They constitute an important class of soft materials. They are characterized by a large amount of solvent, typically ≥98% w/ w, fixed by a small amount of solid
Water-based gels have gained considerable attention over the past 2 decades and turn out to be promising materials for biomedical applications.[1−4] Among the various classes of molecules that have been explored for biocompatible hydrogels, peptides stand out as the material of choice.[1,5,6]
The amino acids obtained through hydrolysis could serve as a nutrient pool
Summary
Gels play an important role in our day-to-day life; toothpaste gels, shaving gels, and shampoos are some of the examples They constitute an important class of soft materials. Depending on the aggregation conditions, the peptide selfassembles to form amyloid-like fibers,[16] nanotubes,[17] and annular rings.[18] The aromatic cassette is believed to play an important role in its self-assembly.[19−22] Phe[19], in particular, is very critical as it resides in the intersheet space and is involved in hydrophobic interactions. Packing of the bulkier Tyr side chain and the possibility of forming hydrogen bonds with water molecules could be the reason These observations led us to investigate the hydrogelating potential of the Phe20Tyr analogue of Aβ16−22.
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