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1.
Bioresour Technol ; 396: 130417, 2024 Mar.
Article in English | MEDLINE | ID: mdl-38316229

ABSTRACT

Global food waste emits substantial quantities of nitrogen to the environment (6.3 Mtons annually), chicken feather (CF) waste is a major contributor to this. Pyrolysis, in particular co-pyrolysis of nitrogen-rich and lignocellulosic waste streams is a promising strategy to improve the extent of pyrolytic nitrogen retention by incorporating nitrogen in its solid biochar structure. As such, this biochar can serve as a precursor for nitrogen-enriched activated carbons for application in supercapacitors. Therefore, this study investigates the co-pyrolysis of CF with macadamia nut shells (MNS) to create nitrogen-rich activated carbons. Co-pyrolysis increased nitrogen retention during pyrolysis from 9 % to 18 % compared to CF mono-pyrolysis, while the porosity was maintained. After removing undesirable inorganic impurities by dilute acid washing, this led to a specific capacitance of 21F/g using a scan rate of 20 mV/s. Finally, cycling stability tests demonstrated good stability with 73 % capacitance retention after 10 000 cycles.


Subject(s)
Charcoal , Macadamia , Refuse Disposal , Animals , Chickens , Nitrogen/chemistry , Feathers , Food , Pyrolysis , Electrodes
2.
Nucleic Acids Res ; 49(14): 7856-7869, 2021 08 20.
Article in English | MEDLINE | ID: mdl-34289065

ABSTRACT

The MYCN gene encodes the transcription factor N-Myc, a driver of neuroblastoma (NB). Targeting G-quadruplexes (G4s) with small molecules is attractive strategy to control the expression of undruggable proteins such as N-Myc. However, selective binders to G4s are challenging to identify due to the structural similarity of many G4s. Here, we report the discovery of a small molecule ligand (4) that targets the noncanonical, hairpin containing G4 structure found in the MYCN gene using small molecule microarrays (SMMs). Unlike many G4 binders, the compound was found to bind to a pocket at the base of the hairpin region of the MYCN G4. This compound stabilizes the G4 and has affinity of 3.5 ± 1.6 µM. Moreover, an improved analog, MY-8, suppressed levels of both MYCN and MYCNOS (a lncRNA embedded within the MYCN gene) in NBEB neuroblastoma cells. This work indicates that the approach of targeting complex, hybrid G4 structures that exist throughout the human genome may be an applicable strategy to achieve selectivity for targeting disease-relevant genes including protein coding (MYCN) as well as non-coding (MYCNOS) gene products.


Subject(s)
DNA/chemistry , G-Quadruplexes , N-Myc Proto-Oncogene Protein/genetics , Nucleic Acid Conformation/drug effects , Small Molecule Libraries/pharmacology , Base Sequence , Cell Line, Tumor , Cell Survival/drug effects , Cell Survival/genetics , Circular Dichroism , DNA/genetics , DNA/metabolism , Gene Expression Regulation, Neoplastic/drug effects , Humans , Ligands , Molecular Structure , N-Myc Proto-Oncogene Protein/metabolism , Neuroblastoma/genetics , Neuroblastoma/metabolism , Neuroblastoma/pathology , Oligonucleotides/chemistry , Oligonucleotides/genetics , Oligonucleotides/metabolism , Small Molecule Libraries/chemistry , Small Molecule Libraries/metabolism , Structure-Activity Relationship
3.
J Submicrosc Cytol Pathol ; 37(3-4): 223-9, 2005 Nov.
Article in English | MEDLINE | ID: mdl-16612971

ABSTRACT

Trypanosoma musculi, a protozoan parasite specific to mouse, was cultured in vitro in the presence of spleen-derived adherent cells. T. musculi co-cultured with adherent cells survived and proliferated indefinitely as long as cellular contact was retained. Scanning and transmission electron microscopy confirmed intimate membrane-to-membrane contact between the adherent cells and parasites. Cellular contact, therefore, seemed to be essential for trypanosomal survival and growth. Immunocytochemical studies demonstrated intense fibroblast growth factor (FGF) activity in adherent cells, and FGFR-2 in associated trypanosomes. BioPorter Lucifer yellow protein delivery reagent studies demonstrated that Lucifer yellow transfected into fibroblast was incorporated into associated trypanosomes. The results suggest the existence of viable channels reminiscent of gap junctions between associated cells. Such transfer of low molecular weight molecules might represent antiapoptotic metabolic factors that support survival of adherent trypanosomes in vitro. Immunocytochemical studies also detected connexin-32 and connexin-43 in the cytoplasm of fibroblasts and associated trypanosomes, however, restriction of connexons to trypanosome/fibroblast adherent sites was not observed. Western blots confirmed the presence of connexin protein molecules in trypanosomes.


Subject(s)
Cell Communication/physiology , Connexins/metabolism , Fibroblasts/microbiology , Fibroblasts/physiology , Trypanosoma/physiology , Animals , Blotting, Western , Cell Adhesion , Coculture Techniques , Connexins/ultrastructure , Electrophoresis, Polyacrylamide Gel , Fibroblasts/ultrastructure , Immunohistochemistry , Isoquinolines , Mice , Microscopy, Electron, Scanning , Microscopy, Electron, Transmission , Receptor, Fibroblast Growth Factor, Type 2/metabolism , Spleen/cytology
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