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1.
Environ Res ; 201: 111502, 2021 10.
Article in English | MEDLINE | ID: mdl-34214561

ABSTRACT

The mycofabricated metal nanoparticles (NPs) plays a significant role in cancer therapeutics and imparts a strategy in medicine. The current investigation focused to synthesize the Copper Oxide Nanoparticles (CuONPs) using an endophytic fungus isolated from Aegle marmelosa medicinal tree located in Western Ghats, India. The endophytic fungus FCBY1 explored the highest antagonistic and antioxidant activities among the 16 pigmented endophytic fungal strains which were isolated from the collected samples. The fungus FCBY1 was identified for its morphological and molecular characteristics where the (Internal Transcribed Spacer) ITS 1, 5.8 ribosomal gene and ITS 2 were sequenced; and the organism FCBY1 is Aspergillus terreus. The endophyte was put through for the synthesis of CuONPs and the size and structure of the synthesized particles were characterized by Scanning Electron Microscope (SEM). The confirmation of the CuONPs was characterized by FT-IR, EDAX and XRD analyses. The CuONPs exhibited the maximized antibacterial and antifungal activities against the human clinical pathogens; moreover the particles also explicated the free radicals/ROS scavenging at minimum concentration, which was assessed through DPPH, nitric oxide radical scavenging assays, and reductive power ability. The anti-cancer activity of CuONPs on colon cancer cell lines (HT-29) was evaluated by MTT (IC50: 22 µg/mL) and FACS analyses (32.11% cells gated in S phase of cell cycle). Angiogenesis inhibition in tumor cells was estimated through in vivo HET- CAM assessment and the highest concentration 60 µL tested inhibited the blood vessels at the percentage of 31.36% and 81.81%. The CuONPs explicated the anti-cancer activities in a concentration - dependent manner and the results of this investigation manifest the significant role of the CuONPs in cancer therapeutics.


Subject(s)
Copper , Metal Nanoparticles , Aspergillus , Fungi , Humans , Microbial Sensitivity Tests , Oxides , Spectroscopy, Fourier Transform Infrared
2.
ACS Appl Bio Mater ; 3(1): 186-196, 2020 Jan 21.
Article in English | MEDLINE | ID: mdl-35019435

ABSTRACT

Although there has been considerable achievement in the field of breast cancer therapeutics, tackling the disturbing issue of highly potent triple-negative breast cancer (TNBC) still remains a hurdle in cancer therapeutics. Here, for the first time we propose a poly(ethylenimine) (PEI)-mediated approach for the synthesis of hyaluronic acid (HA) tagged cerium oxide nanoparticles (CePEI-NPs) as a therapeutic agent in TNBC. Primarily, the formulated HA-CePEI-NPs upon treatment displayed superior anticancer effect by exhibiting the loss of mitochondrial membrane potential (MMP). These particles acted as a nano reactor by the generation of reactive oxygen species (ROS) during the treatment. We further evaluated the caspase activity which divulgated the activation of caspases-3 and -9 while there was a decrease in the level of Bcl-2. The treatment also resulted in the release of cytochrome c (Cyt c), and in addition, features such as pynknosis and G2/M phase arrest were also noted. Hence the nano reactor property of nano ceria in activating mitochondrial-mediated intrinsic apoptosis highlights its promising role as a nano drug for therapeutic applications in TNBC.

3.
Appl Microbiol Biotechnol ; 100(11): 4779-89, 2016 Jun.
Article in English | MEDLINE | ID: mdl-27094187

ABSTRACT

Pterin deaminase is an amidohydrolase enzyme hydrolyzing pteridines to form lumazine derivatives and ammonia. The enzyme captured the attention of scientists as early as 1959 and had been patented for its application as an anticancer agent. It is ubiquitously present in prokaryotes and has been reported in some eukaryotes such as honey bee, silkworm and rats. The enzyme has been observed to have a spectrum of substrates with the formation of respective lumazines. The role of the substrates of the enzyme in various metabolic pathways warrants a significant role in the biological activity of both prokaryotes and eukaryotes. Even though the functions of the enzyme have been explored in prokaryotes, their niche in the eukaryotic system is not clear. There is very few information on the structural and functional properties of the enzyme. This review has been congregated to emphasize the significance of pterin deaminase and analyzes the lacunae in understanding the biological characters of the enzyme.


Subject(s)
Amidohydrolases/metabolism , Aminohydrolases/metabolism , Aminohydrolases/antagonists & inhibitors , Animals , Biopterins/analogs & derivatives , Biopterins/metabolism , Eukaryotic Cells/enzymology , Prokaryotic Cells/enzymology , Pteridines/chemistry
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