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https://www.selleckchem.com/products/abt-199.html Collagen, the most abundant protein in mammals, possesses notable cohesion and elasticity properties and efficiently induces tissue regeneration. The Gly-Pro-Hyp canonical tripeptide repeating unit of the collagen superhelix has been well-characterized. However, to date, the shortest tripeptide repeat demonstrated to attain a helical conformation contained 3-10 peptide repeats. Here, taking a minimalistic approach, we studied a single repeating unit of collagen in its protected form, Fmoc-Gly-Pro-Hyp. The peptide formed single crystals displaying left-handed polyproline II superhelical packing, as in the native collagen single strand. The crystalline assemblies also display head-to-tail H-bond interactions and an "aromatic zipper" arrangement at the molecular interface. The coassembly of this tripeptide, with Fmoc-Phe-Phe, a well-studied dipeptide hydrogelator, produced twisted helical fibrils with a polyproline II conformation and improved hydrogel mechanical rigidity. The design of these peptides illustrates the possibility to assemble superhelical nanostructures from minimal collagen-inspired peptides with their potential use as functional motifs to introduce a polyproline II conformation into hybrid hydrogel assemblies.Ferroelectric materials have drawn widespread attention due to their switchable spontaneous polarization and anomalous photovoltaic effect. The coupling between ferroelectricity and the piezo-phototronic effect may lead to the design of distinctive photoelectric devices with multifunctional features. Here, we report an enhancement of the photovoltaic performances in the ferroelectric p-type La-doped bismuth ferrite film (BLFO)/n-type zinc oxide (ZnO) nanowire array heterojunction by rationally coupling the strain-induced piezoelectricity in ZnO nanowires and the ferroelectricity in BLFO. Under a compressive strain of -2.3% and a 10 V upward poling of the BLFO, the open-circuit voltage (VOC) and sho
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