muramidase and cinnamaldehyde

Amyloidosis is the process of fibril formation responsible for causing several diseases in the human being that involve protein aggregation such as Alzheimer's, Parkinson's, Huntington's disease, and type II diabetes. Natural phytocompounds such as curcumin shown promising anti-amyloidogenic activity. In the present study, selective phytocompounds such as piperine, cinnamaldehyde, eugenol, and cuminaldehyde present in Piper nigrum L, Cinnamomum zeylanicum Blume, Eugenia caryophyllus Thumb, and Cuminum cyminum L, respectively were analyzed for anti-amyloidogenic activity using hen egg white-lysozyme (HEWL) as a model system. Out of the selected phytocompounds, piperine showed the most significant anti-amyloidogenic activity, as evident from in vitro assays that were validated by in silico molecular docking study. Piperine showed 64.7 ± 3.74% inhibition of amyloid formation at 50 μM concentration, as observed by Thioflavin T assay. Subsequently, the anti-amyloidogenic activity of piperine was further validated by congo red, intrinsic fluorescence assay, and transmission electron microscopy analysis. The in silico molecular binding interaction showed piperine with the highest docking score and glide energy. Piperine was found to be interacting with amyloidogenic region residues and Trp62, the most important residue involved in the amyloidogenesis process. In conclusion, piperine can be used as a positive lead for a potential therapeutic role in targeting diseases involved amyloidogenesis.

Topics: Acrolein; Alkaloids; Amyloidogenic Proteins; Animals; Benzaldehydes; Benzodioxoles; Benzothiazoles; Binding Sites; Chickens; Cymenes; Eugenol; Fluorescent Dyes; Humans; Molecular Docking Simulation; Muramidase; Phytochemicals; Piperidines; Polyunsaturated Alkamides; Protective Agents; Protein Aggregates; Protein Binding; Protein Interaction Domains and Motifs; Protein Structure, Secondary; Spectrometry, Fluorescence

The effect of cinnamaldehyde (CM) enriched diet on immunity and cytokine gene expression in Channa striatus against Aphanomyces invadans is reported. C. striatus was uniformly divided into eight groups (n = 25 fish each) and fed with formulated diets with 0, 5, 10, and 15 mg kg

Topics: Acrolein; Animals; Aphanomyces; Complement Activation; Diet; Fish Diseases; Fishes; Gene Expression; Immunity, Innate; Immunoglobulin M; Infections; Leukocyte Count; Muramidase; Phagocytosis; Reactive Oxygen Species

Effects of lysozyme (LYS) combined with cinnamaldehyde (CA) on quality enhancement of olive flounder (Paralichthys olivaceus) fillets during refrigerated storage at 4 °C for 20 days were assessed. Changes of total viable count (TVC), K-value, total volatile basic nitrogen (TVB-N), thiobarbituric acid (TBA), texture profile analysis (TPA), and trichloroacetic acid-soluble peptide (TCA-soluble peptide) in samples were determined periodically. Results demonstrated that the combination of LYS and CA treatment enhanced the antibacterial activity against S. putrefaciens and P. fluorescens, and lowered TVC values. Meanwhile, LYS combined with CA significantly retarded the increases of TBA value, TVB-N, K-value, and TCA-soluble peptide content compared to the control. Furthermore, the combined treatment also effectively maintained the texture properties of flounder fillets during the storage period. The efficiency was better than that of LYS or CA treatment alone. Thus, LYS combined with CA is promising in olive flounder shelf life extension.

Topics: Acrolein; Animals; Fish Products; Flatfishes; Food Preservation; Food Preservatives; Food Storage; Muramidase; Nitrogen

Numerous efforts have been directed towards investigating the different stages leading to the fibrillation process in neurodegenerative diseases and finding the factors modulating it. In this study, using a wide range of molecular techniques as well as fibrillation kinetics coupled with differential scanning fluorimetry (DSF) and crystal structure determination of HEWL treated with cinnamaldehyde (Cin) and Phenyl ethyl alcohol (PEA) in their aroma form during fibrillation, we were able to identify the binding positions of Cin and PEA in HEWL. Additionally, crystal structures were used to suggest residues Thr43, Asn44, Arg45 and Arg68 as a plausible 'hotspot' promoting entrapment of intermediate species in the process of fibril formation in HEWL. We were also able to use DSF to show that Cin can significantly decrease the thermal stability of HEWL, promoting the formation of partially unfolded intermediate species. In conclusion, our data led us to emphasize that compounds in their 'aroma form' can influence the structure and stability of protein molecules and suggest reconsideration of HEWL as a model protein for fibrillation studies related to neurodegenerative diseases based on the initial structure of the proteins, whether globular (HEWL) or intrinsically disordered.

Topics: Acrolein; Animals; Binding Sites; Chickens; Circular Dichroism; Hot Temperature; Kinetics; Muramidase; Neurodegenerative Diseases; Phenol; Phenylethyl Alcohol; Protein Binding; Protein Denaturation; Protein Folding; Static Electricity