No abstract

Peptide-based drugs have become the most promising drug therapy in the pharmaceutical industry. It accommodates a major part in treating diseases like neurodegenerative disorders, type 2 diabetes, blood pressure, etc. This study aims to isolate and characterize the marine peptides from the crustacean crab species named Scylla Serrata. The hemolymph was collected and subjected to thin-layer chromatography (TLC) and Fourier Transform Infrared spectroscopy for identifying amine groups. Further the peptide groups in the sample was confirmed by nuclear magnetic resonance analysis. Ultra-performance liquid chromatography (UPLC) for the crude was performed to identify the intensity of the peaks. The sample was further purified with Sephadex G-25 to elute the small molecular peptides. Antioxidant activity (DPPH) for the crude sample showed 55% of activity at 100µg/ml concentration and the fractions showed significant activity. The eluted fractions from the column chromatography were then subjected to SDS PAGE to identify the molecular weight of the peptides in which the peptide bands ranged between 75–100 kDa. Further, the best compounds must be developed as potential drugs for Alzheimer’s disease with an In-silico approach.

In this study, the antimicrobial effect and DNA gyrase inhibitor potential of vanillin-based pyridyl-substituted fluoro-indolines were evaluated. These compounds are synthesized and established through green-chemistry approaches.The inhibition effect on both DNA gyrase A and B was evaluated in silico and in vitro. Agar well diffusion method-based antimicrobial activity against Gram-ve Pseudomonas aeruginosa (MTCC 424) and Escherichia coli (MTCC 443), Gram+ve Streptococcus pyogenes (MTCC 442) and Staphylococcus aureus (MTCC 96), and a clinical isolate of Candida albicans (Fungi) was evaluated.The cytotoxicity of the compounds was assessed over macrophages using the MTT assay. In the results, the target compounds exhibited a broad-spectrum antimicrobial activity against both bacterial types and fungal.

We aimed to design and develop short peptide inhibitors targeting Low-Density Lipoprotein receptor-related Protein 6 (LRP6) as a therapeutic for Alzheimer’s disease (AD). Considering the critical association of LRP6 co-receptor with Dickkopf-related protein 1 (DKK1), which is majorly involved in the upregulation of AD via canonical Wnt signaling. After assessing the critical amino acid residue involved in the DKK1-LRP6 complex, a 16-amino acid (16aa) length short peptide was retrieved to be used as the inhibitory peptide. Further, using alanine scanning, we generated 16 different mutated peptides and their binding potential in-silico to LRP6, which ensured the blockage of the DKK1 association to LRP6. Further, the peptides were subjected to envisage their toxicity, physicochemical properties, and ADMET properties. In the results, apart from the native inhibitory peptide (16aa), the mutated peptides 16aa8, 16aa1, 16aa7, and 16aa6 showed good binding with LRP6 which made the blockage of DKK1 association to LRP6. As a future perspective, the top-scored peptides including the native peptides will be screened for synthesizing characterizing, and validating their in vitro and in vivo therapeutic potential to treat AD through the DKK1 inhibition mechanism.