Lignin is the main constituent of lignocellulosic biomasses, which have a significant untapped ability to replace ecologically unfavorable and non-renewable fossil fuels. The lignin is broken down by ligninolytic bacteria, which also use a peripheral pathway to transform heterogeneous lignin derivatives into central intermediates like protocatechuate or catechol. By undergoing ring cleavage through the -ketoadipate pathway, these intermediates become metabolites by producing acetyl-CoA for internal product biosynthesis, including the creation of triacylglycerols and polyhydroxyalkanoates. Expanding our understanding of ligninolytic microbial communities, strains, and enzymes through bioprospecting can help us better understand the metabolism of aromatics. The most viable idea for sustainable development is the valorization of lignin into biopolymers as well as other high-value goods. This process is now being used to generate a variety of biopolymers, including polyesters, epoxies, phenol resins, poly (lactic acids), poly hydroxyl alkanoates, and polyurethanes. Furthermore, lignin recalcitrance remained a possible barrier to efficient lignin valorization, prompting several efforts to design high-efficiency bioprocesses to produce specific polymer types as well as other important bioproducts. Graphical Abstract
Targeted delivery of therapeutic anticancer chimeric molecules enhances the efficacy of drug by improving cellular uptake and circulation time. Engineering the molecules to facilitate the specific interaction between chimeric protein and its receptor is critical to elucidate biological mechanism as well as accuracy in modeling of complexes. A theoretically designed novel protein-protein interfaces can serve as a bottom-up method for comprehensive understanding of interacting protein residues. This study was aimed for in silico analyses of a chimeric fusion protein against breast cancer. The amino acid sequences of the interleukin 24 (IL-24) and LK-6 peptide were used to design the chimeric fusion protein via a rigid linker. The secondary and tertiary structures along with physicochemical properties by ProtParam and solubility were predicted using online software. The validation and quality of the fusion protein was confirmed by Rampage and ERRAT2. The newly designed fusion construct has a total length of 179 amino acids. The top-ranked structure from alpha fold2 showed 18.1 KD molecular weight by ProtParam, quality factor of 94.152 by ERRAT, and a valid structure by a Ramachandran plot with 88.5% residues in the favored region. Finally, the docking and simulation studies were performed using HADDOCK and Desmond module of Schrodinger. The quality, validity, interaction analysis, and stability of the fusion protein depict a functional molecule. The fusion gene IL24-LK6 after cloning and expression in a suitable prokaryotic cell might be a useful candidate for developing a novel anticancer therapy.
Different plants respond to photoperiod in diverse manners. There are three major types of the responses of photoperiodism in plants: short-day responses (SD), long-day responses (LD) and dayneutral responses (DN). The LD plants flower most rapidly under high intensity of light provided for a large period of time while the short day plants flower rapidly only if light is provided for a short period of time. The plants with day-neutral responses, does not depends on the conditions of photoperiod in order to flower. Every plant behaves according to the length of light on its own way. In this study the plants that were considered shows distinct responses. Lettuce (Lactuca sativa), for example responded towards longday photoperiod. Synthetic hexaploids showed a slight photoperiodic response of Triricum turgidum rather than the accessions of Triticum tauschii. Tomato (Solanum Lycopersicum) showed a day neutral response but some modern tomatoes had mild short day response towards photoperiodism. The tuberization in potato (Solanum tuberosum) was favored by short day photoperiodic response as well as cool temperature.
Epidermal growth factor receptor (EGFR), a member of HER receptor family is over expressed in various cancer cells. Using tumor-specific antibodies to deliver cytotoxic agents directly to the tumor cells is an effective treatment strategy. Targeted therapy by fusing anti-EGFR scfv with tumor specific cytokines promises the emergence of new era. We designed a novel immuno-apoptotic fusion protein, anti EGFR Scfv-IL-24, consisting of a specific cancer cell targeting antibody and recombinant cytokine IL-24 to explore its anti-cancerous potential. Amino acid sequences of both anti EGFR scfv and IL-24 were fused using specific rigid linker. In silico characterization of the designed fusion protein like to predict the primary, secondary, physiochemical properties, quality and structural validation using online bioinformatic tools. Newly designed fusion protein consists of 402 amino acids that showed good quality with predicted value of 76.7% having 81.5% residues in most favored region as predicted by ERRAT2 and Ramachandran plot analysis. Docking and simulation studies were performed using HDOCK and Desmond module of Schrodinger. All the parameters of quality, validity, interaction analysis and stability suggested that the fused molecule is fully operational and functional. The results of the study supports that the anti EGFR Scfv-IL-24 fused protein could be proved as a novel candidate to combat cancer.
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