Project description:Clitoria ternatea L. commonly known as 'blue pea' is an underutilized plant in Sri Lanka. The blue coloured flower of this plant is used in medicine in Sri Lankan traditional medical system and also reported to have several health benefits in recent findings at the international level. However, to date scientifically validated value added products from blue pea flower (BPF) is very limited worldwide. In this connection, this study was carried out to develop a commercial potential blue pea flower extract (BFE) incorporated beverage having functional properties. Dried BPFs were extracted into water with varying flower: water ratio, temperature, and time using response surface methodology (RSM) along with Box-Behnken design. A range of BFE incorporated beverages was developed comprising a natural sweetener (Stevia extract) and a flavour (lime). The most acceptable formulation was selected via ranking and hedonic sensory tests. Further, it was evaluated for functional properties in terms of antioxidant activity via total polyphenolic and flavonoid contents, ferric reducing antioxidant power and radical scavenging activities via ORAC; DPPH and ABTS. Glycaemic regulatory properties (GCP) were evaluated in terms of antiamylase and antiglucosidase activities. Quality parameters of the developed beverage were evaluated for a period of 28 days at different time intervals and a colour chart was also developed. The optimum conditions for extraction of BPF via RSM were 3 g of powdered BPF/L of water at 59.6 °C for 37 min. The most acceptable formulation consists of BFE, Stevia extract, and lime at a ratio of 983.25:1.75:15. Further, it had significantly higher (p<0.05) consumer preference for sensory attributes. Further, it possesses an antioxidant activity through multiple mechanisms while GCP were not detected. Moreover, it was shelf stable for a period of 28 days without preservatives. The colour chart can be used to monitor the quality of the beverage.
Project description:Objectives: In this study, we implemented a structure-based virtual screening protocol in search of natural bioactive compounds in Clitoria ternatea that could inhibit the viral Mpro. Methods: A library of twelve main bioactive compounds in C. ternatea was created from PubChem database by minimizing ligand structure in PyRx software to increase the ligand flexibility. Molecular docking studies were performed by targeting Mpro (PDB ID: 6lu7) via Discovery Studio Visualiser and PyRx platforms. Top hits compounds were then selected to study their Adsorption, distribution, metabolism, excretion, and toxicity (ADMET) and drug likeness properties through pkCSM pharmacokinetics tool to understand the stability, interaction, conformational changes, and pharmaceutical relevant parameters. Results: This investigation found that, in the molecular docking simulation, four bioactive compounds (procyanidin A2 [−9.3 kcal/mol], quercetin-3-rutinoside [−8.9 kcal/mol], delphinidin-3-O-glucoside [−8.3 kcal/mol], and ellagic acid [−7.4 kcal/mol]) showed producing the strongest binding affinity to the Mpro of severe acute respiratory syndrome coronavirus 2, as compared to positive control (N3 inhibitor) (−7.5 kcal/mol). These binding energies were found to be favorable for an efficient docking and resultant. In addition, the stability of quercetin-3-rutinoside and ellagic acid is higher without any unfavorable bond. The ADMET and drug likeness of these two compounds were found that they are considered an effective and safe coronavirus disease 2019 (COVID-19) inhibitors through Lipinski’s Rule, absorption, distribution, metabolism, and toxicity properties. Conclusion: From these results, it was concluded that C. ternatea possess potential therapeutic properties against COVID-19.
Project description:Flowers of the butterfly pea (Clitoria ternatea) accumulate a group of polyacylated anthocyanins, named ternatins, in their petals. The first step in ternatin biosynthesis is the transfer of glucose from UDP-glucose to anthocyanidins such as delphinidin, a reaction catalyzed in C. ternatea by UDP-glucose:anthocyanidin 3-O-glucosyltransferase (Ct3GT-A; AB185904). To elucidate the structure-function relationship of Ct3GT-A, recombinant Ct3GT-A was expressed in Escherichia coli and its tertiary structure was determined to 1.85 Å resolution by using X-ray crystallography. The structure of Ct3GT-A shows a common folding topology, the GT-B fold, comprised of two Rossmann-like β/α/β domains and a cleft located between the N- and C-domains containing two cavities that are used as binding sites for the donor (UDP-Glc) and acceptor substrates. By comparing the structure of Ct3GT-A with that of the flavonoid glycosyltransferase VvGT1 from red grape (Vitis vinifera) in complex with UDP-2-deoxy-2-fluoro glucose and kaempferol, locations of the catalytic His-Asp dyad and the residues involved in recognizing UDP-2-deoxy-2-fluoro glucose were essentially identical in Ct3GT-A, but certain residues of VvGT1 involved in binding kaempferol were found to be substituted in Ct3GT-A. These findings are important for understanding the differentiation of acceptor-substrate recognition in these two enzymes.