The application of natural dye in the textile industry is gaining popularity because of the increasing awareness of environmental effects, the ecological effects, and the pollution caused by synthetic dyes. Rose flowers, which are one of the best sources of natural dye, have been selected for fabric dyeing due to the presence of anthocyanin pigment. Dyeing of wool is done at optimal conditions such as pH, temperature, time, and salt. It is found that at different percentages (1%, 3%, 5%, 7%, and 9%) chemical and bio mordants mediums gave a variety of shades of good color and better fastness properties onto natural fabrics. By using different chemical and bio mordants and their combinations to analyze the color strength and fastness properties could be enhanced. Bio-mordants gave shades with good color strength and acceptable for the universe. The plant extract has therapeutic values like antioxidant, anti-inflammatory, and antibacterial activity against some gram-positive and gram-negative pathogenic bacteria.

Natural products have gained worldwide favor due to their sustainable and ayurvedic nature. In this study, rose containing anthocyanin was explored as a source of yellowish–pink natural colorant for wool dyeing using various solvents (aqueous, alkaline, acidic, and basified methanol). Dyeing of wool was performed by optimizing the following parameters: pH, temperature, time, and salt concentration. It was observed that aqueous extract with a pH of 3 employed at 80 °C for 35 min with the addition of 4 g/100 mL salt, acidic extract with a pH of 2 employed at 40 °C for 35 min with the addition of 2 g/100 mL salt, alkaline extract with a pH of 1 employed at 80 °C for 45 min with the addition of 3 g/100 mL salt, and methanolic extract with a pH of 2 employed at 80 °C for 45 min with the addition of 4 g/100 mL salt resulted in high tint (K/S) values. To improve the colorfastness properties, salts of iron (Fe⁺²), aluminum (Al⁺³), and tannic acid (Tn) were used as chemical mordant, whereas turmeric and pomegranate were used as biomordants. Iron (Fe⁺²) and pomegranate resulted in shades with good colorfastness characteristics. The plant extract and dyed fabrics were also evaluated against Gram-positive and Gram-negative bacteria Staphylococcus aureus and Escherichia coli, respectively, to observe their antibacterial potential. The results indicate that wool fabric dyed with naturally sourced rose petals can be used as valuable antibacterial fabric due to the presence of various bioactive compounds by dissipating the effect of allergy-causing synthetic dyed fabrics.

Maize is a vital cereal crop, severely affected by environmental factors and climate change. Among abiotic factors, drought stress is considered one of the most detrimental factors limiting plant growth and biomass production. However, the molecular basis of bacterial metabolite-mediated drought tolerance in cereal crops remains poorly understood. The current in silico study aimed to investigate the molecular interactions between Kocuria oceani AT-1 metabolites and the maize UGT706F8 protein, using molecular docking and dynamics simulation analyses. The molecular interactions between bacterial metabolites and the UGT706F8 protein (glycosyltransferase enzyme, PDB ID 7Q3S) from Zea mays L. were evaluated. The in silico docking findings revealed a favorable binding affinity between bacterial metabolites and the target protein, indicating stable molecular interactions at the protein active site. Specifically, 4-tetradecanoyl-2,6-piperazinedione, and 3-benzylhexahydropyrrolo(1,2-a)pyrazine-1,4-dione displayed binding energies of −7.5 ± 0.33 and −8.5 ± 0.36 kcal/mol against the target protein, respectively. Under identical docking parameters, the known plant growth regulators (indole acetic acid and abscisic acid) yielded binding energies of −6.6 ± 0.34 and −5.8 ± 0.32 kcal/mol, respectively. Re-docking of the native uridine-5-diphosphate (UDP) ligand yielded a Root Mean Square Deviation (RMSD) of 0.9 Å, validating the reliability of the docking procedure. Additionally, molecular dynamics simulation (200 nanoseconds) outcomes supported these predictions, indicating stable molecular interactions and structural integrity of ligand-protein complexes, with ligand RMSD values remaining between 2 and 3 Å. The formation of hydrogen bonding (an average of 2.4 ± 0.6 and 2.1 ± 0.5, respectively), hydrophobic interactions, and stable Solvent-Accessible Surface Area (SASA) profiles (ranging between 19,000–22,000 Å ² and 19,000–21,000 Å ² , respectively) suggest the stability of complexes. Moreover, Molecular Mechanics Generalized Born Surface Area (MM-GBSA) outcomes (−102.05 ± 13.96 and −54.86 ± 7.93 kcal/mol, respectively) supported the favorable binding energetics of ligand-protein complexes. These computational outcomes suggest that Kocuria oceani metabolites can establish stable molecular interactions with the UGT706F8 protein, which may influence glycosyltransferase function. Further in vivo experimental validation is required to confirm their predicted maize growth-promoting potential under drought conditions.

Despite the current development and progress in vaccine synthesis, the transmission and infection rate of new variants of SARS-CoV-2 is still challenging in developing countries like Pakistan. Previous studies reported the transmission of new virus variants associated with the mutation in spike protein particularly in the receptor binding domain (RBD) of SARS-CoV-2 making RBD a promising target to control the infection rate. Any change in the spike RBD affects the interaction with host angiotensin-converting enzyme 2 (hACE2) receptor. These mutations in RBD assist SARS-CoV-2 entry in the host and enhance virulence and transmission rate. In the current study, we retrieved all substitution mutations in RBD of spike protein in three Pakistani SARS-CoV-2 variants from the GISAID database. Their structures were predicted via ColabFold2 and protein-protein docking was performed using HADDOCK. Interactions between docked complexes were checked by PyMOL and binding affinity (ΔG) (kcal/mol) was calculated via Prodigy server. The results of protein-protein interaction showed that the mutated hCoV-12471804 variant exhibited a higher number of interactions (202), low Z-score (−2.1), increased buried surface area (4066.4 ± 55.9), and high binding affinity (−21.3 kcal/mol) with hACE2 compared to hCoV-Wild variant. Moreover, the current study provides insights into the effects of mutations in RBD with hACE2 interaction providing deeper structural insight to understand the molecular mechanism responsible for the increased transmissibility of newly emerged SARS-CoV-2 variants. The exclusively in silico nature of this study necessitates experimental validation to definitively quantify the kinetic and thermodynamic parameters of the hACE2-RBD interaction.