Sensitising natural wool with green and brown coffee using a facile extraction method to optimise dye process parameters.

Green coffee powder is the raw powder of coffee cherries and all coffee's potential components are held within this green powder. A new natural colourant was extracted from Green Coffee using water as an extractant. To obtain a green-colored solution, a specific amount of green coffee was mixed with distilled water and left for 24 h at room temperature. Furthermore, the colouring performance of extracted colour has been studied using the conventional exhaust dyeing method on wool fabric. Different parameters viz. concentration of Green coffee powder, the temperature of the dye bath, the period for immersion, and solution pH were made to set to obtain a fine tone of green colour. The dyeing parameters (amount of the coffee: 2 g, 100 °C, 70 min & 6.7 pH) were optimised and selected to draw a comparison with the conventional Brown coffee powder. In experiments on wool, this potential solution of Green coffee offered rich green hues with good tonal variation. In addition, the colour fastness to washing was found superior in the case of both Green and Brown coffee and colour fastness to light, rubbing as well as perspiration also showed good performance. In this study, our main focus was to obtain the true and fast green tone of the fabric using Green Coffee and compare it with brown coffee using the same conditions used for dyeing with green coffee. The application of these dyes as natural dyes results in obtaining innovative natural fast colour with remarkable dyeing properties and a new inclusion to the existing commercial spectra of natural dyes.

Proline based rationally designed peptide esters against dipeptidyl peptidase-4: Highly potent anti-diabetic agents.

With the target to develop small molecules based anti-diabetic agents, we, herein, report the design, synthesis and biological studies on Lys-Pro and Gly-Pro esters, and a Phe-Pro-Phe tripeptide inhibiting the activity of glycoprotein dipeptidyl peptidase-4 (DPP-4). Since DPP-4 cleaves the glucagon like peptide (GLP-1) and glucose dependent insulinotropic polypeptide (GIP) hormones which are responsible for inducing insulin secretion, the results of present studies could be significant in making control over glycemia. The structural analysis of DPP-4 and its binding mode with the substrate as well as the reported inhibitors provided the background for the design of new molecules. Among the 17 compounds screened against DPP-4, 14 compounds displayed IC50 better than the known drug Sitagliptin. Collectively, a highly encouraging set of molecules was identified that may prove as the clinical candidates for the treatment of diabetes.