Isolation, characterization and anti-inflammatory activity of compounds from the Vernonia amygdalina.

The need to explore the abundance of natural products cannot be overemphasized particularly in the management of various disease conditions. In traditional medical practice, Vernonia amygdalina has been widely adopted in the management of various inflammatory disorders. The objective of this investigation was to isolate the bioactive principles from the stem-bark and root of V. amygdalina and assess the anti-inflammatory (in vitro) activity of both the crude extracts and the isolated compounds. Following extraction with the methanol, the extract was subjected to gravity column chromatography and the resultant fractions was further purified to obtained pure compounds. The structural elucidation of the compounds were based on data obtained from 1H to 13C nuclear magnetic resonance (NMR) spectroscopies as well as fourier transform infrared (FT-IR). Using diclofenac as a control drug, the albumin denaturation assay was used to determine the in vitro anti-inflammatory activity of the extracts and isolates. Three distinct compounds characterized are vernoamyoside D, luteolin-7-α-o-glucuronide, and vernotolaside, a new glycoside. When compared to diclofenac, which has an IC50 of 167.8 µg/mL, luteolin-7-α-o-glucuronide, vernoamyoside D, and vernotolaside all showed significant inhibitions with respective IC50 values 549.8, 379.5, and 201.7 µg/mL. Vernotolaside is reported for the first time from the root. The assertion that the plant is used in traditional medicine for the management of inflammatory disorder is somewhat validated by the confirmation of the existence of the compounds with the biochemical actions. Further validation of the isolated compounds would be required in animal studies.

Effect of the spacer on the structure and self-assembly of FF peptide mimetics.

We have designed and synthesized a series of FF peptide mimetics with conformationally rigid and flexible spacers to study the effect of spacers on their structure and self-assembly. The results help in understanding biomolecular aggregation and provide a strategy to obtain fractal pattern materials. From X-ray single crystal analysis, the m-diaminobenzene appended FF peptide mimetic adopts a duplex structure stabilized by multiple intermolecular hydrogen bonds. There is also a water molecule bridging between two strands of the duplex. Moreover, the duplex is stabilized by three face-to-face, face-to-edge and edge-to-edge π-π interactions. The duplex formation is also supported by mass spectrometry. In higher order packing, the dimeric subunits further self-assembled to form a complex sheet-like structure stabilized by multiple intermolecular hydrogen bonding and π-π stacking interactions. Moreover, the 1,4-butadiene and m-xylylenediamine appended FF peptide mimetics form stimuli-responsive organogels in a wide range of solvents including methanol. The rheology data of FF peptide mimetic gels as a function of angular frequency and oscillatory strain also supported the formation of strong physically crosslinked gels. The FE-SEM images of the xerogels obtained from different organic solvents show that the network morphology of FF peptide mimetics varies depending on the nature of the solvents.

Synthesis and Structural Investigation of Foldamer-Based Iodine-Supported Artificial Glycosidases.

Glycosidases are a type of enzyme that hydrolytically cleave carbohydrates and form glycans for biologically important processes. The inadequacies of glycosidases or their genetic abnormalities are responsible for various diseases. Thus, the development of glycosidase mimetics is of great importance. We have designed and synthesized an enzyme mimetic containing l-phenylalanine, α-aminoisobutyric acid (Aib), l-leucine, and m-Nifedipine. From X-ray crystallography, the foldamer adopts a ß-hairpin conformation stabilized by two 10-member and one 18-member NH⋅⋅⋅O=C hydrogen bonds. Moreover, the foldamer was found to be highly efficient in hydrolysing ethers and glycosides in the presence of iodine at room temperature. Further, X-ray analysis shows the backbone conformation of the enzyme mimetic to be almost unchanged after the glycosidase reaction. This is the first example of iodine-supported artificial glycosidase activity with an enzyme mimic at ambient conditions.

α,ε-Hybrid Peptide-Stabilized Magnetic Nanoparticle-Coated Paper-Based Actuators.

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.