The self-assembly, organogelation, syneresis, and anti-adhesion properties of a Peptidomimeticcontaining L-phenylalanine and 2,6-dimethylpyridine 3,5-dicarboxylic acid have been studied in detail. The peptidomimetic forms a transparent gel in aromatic solvents such...

We have designed and synthesized a series of FF peptide mimetic with conformationally rigid and flexible spacers to study the effect of spacers on their structure and self-assembly. The results...

The development of α,ε-hybrid peptide-stabilized magnetic nanoparticles and their application to fabricate a paper-based actuator has been reported. From single-crystal diffraction analysis, the nitropeptide 2 has an extended structure with a trans geometry. The one-pot in situ multiple oxidation–reduction reaction of a synthetic nitropeptide solution in ammonium hydroxide and FeCl2 leads to the formation of Fe3O4 nanoparticles. The reduction reaction replaces the nitro group with an amine group, which finally acts as capping agent for the stabilization of the Fe3O4 nanoparticles. Paper-based soft magneto machines with multivariant actuation modes such as contraction–expansion, bending, and uplifting locomotion have been studied. The device has potential as controllable paper-based soft robots.

Benzotriazole esters have been reported to work as inactivators for severe acute respiratory syndrome (SARS) 3CL protease. A calcium channel blocker m‐Nifedipine is well known for its effect in hypertension, as well as angina. Combining two, we have synthesized co‐drug m‐Nifedipine‐3‐benzotriazol‐1‐yl‐ester 1 which exhibited antifungal activities against Saccharomyces cerevisiae (S. cerevisiae strain BY4742). The single‐crystal X‐ray diffraction study shows that there are two molecules with opposite chirality in the asymmetric unit. Intramolecular π‐π stacking interactions stabilize the tripod shape compound 1 molecules. In higher‐order assembly, compound 1 molecules are assembled by intermolecular hydrogen bonding, maintaining a proper registry to form a supramolecular nanotube‐like structure. Moreover, compound 1 inhibits the growth of the Saccharomyces cerevisiae. The minimal inhibitory concentration (MIC) against the Saccharomyces cerevisiae was 10 μg/mL. The docking studies indicate that compound 1 has a strong affinity (binding energy −8.67 kcal/mol) for the enzyme lanosterol 14α‐demethylase of the Saccharomyces cerevisiae. The compound 1 binds to Leu58 and Ser50 of lanosterol 14α‐demethylase through intermolecular hydrogen bonding interactions.

This paper reports a stimuli-responsive designer supramolecular polymer gel in dimethylsulphoxide (DMSO)/water (1:2) based on a dipeptide amphiphile and β-cyclodextrin (β-CD) The dipeptide amphiphile contains caproic acid at the N terminus and methyl ester at the C terminus. From X-ray single crystal diffraction, the amphiphile adopts a kink-like conformation. The amphiphile self-assembled to form a parallel sheet-like structure stabilized by multiple intermolecular hydrogen bonds. Moreover, the parallel sheet-like structure is also stabilized by edge-to-edge π–π stacking interactions. In higher-order packing, it forms a corrugated sheet-like structure stabilized by hydrophobic interactions. The dipeptide amphiphile interacts with β-cyclodextrin and forms gel through supramolecular polymer formation in (DMSO)/water (1:2) by a simple heating-cooling cycle. The sol-to-gel transformation is because of a host–guest complex between compound 1 and β-CD and the formation of supramolecular polymer accompanied by microstructure changes from nanofibers to microrods. The gel is temperature responsive with a Tgel of 70 °C. The supramolecular polymer gel is also responsive to stimuli such aspicric acid and HCl. The extensive spectroscopic studies show that the aromatic hydrophobic side chain of compound 1 forms a host–guest complex with β-CD. These results will be helpful for the design of advanced programable eco-friendly functional materials.