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1.
Int J Mol Sci ; 24(15)2023 Jul 28.
Article in English | MEDLINE | ID: mdl-37569487

ABSTRACT

This study aimed to evaluate Attalea funifera seed oil with or without resveratrol entrapped in organogel nanoparticles in vitro against A375 human melanoma tumor cells. Organogel nanoparticles with seed oil (SON) or with resveratrol entrapped in the seed oil (RSON) formed functional organogel nanoparticles that showed a particle size <100 nm, polydispersity index <0.3, negative zeta potential, and maintenance of electrical conductivity. The resveratrol entrapment efficiency in RSON was 99 ± 1%. The seed oil and SON showed no cytotoxicity against human non-tumor cells or tumor cells. Resveratrol at 50 µg/mL was cytotoxic for non-tumor cells, and was cytotoxic for tumor cells at 25 µg/mL. Resveratrol entrapped in RSON showed a decrease in cytotoxicity against non-tumor cells and cytotoxic against tumor cells at 50 µg/mL. Thus, SON is a potential new platform for the delivery of resveratrol with selective cytotoxic activity in the treatment of melanoma.


Subject(s)
Antineoplastic Agents , Arecaceae , Melanoma , Nanogels , Nanoparticle Drug Delivery System , Palm Oil , Resveratrol , Resveratrol/administration & dosage , Melanoma/therapy , Humans , Cell Line, Tumor , Nanogels/administration & dosage , Nanogels/chemistry , Arecaceae/chemistry , Palm Oil/chemistry , Seeds/chemistry , Particle Size , Antineoplastic Agents/administration & dosage , Antineoplastic Agents/chemistry
2.
Nat Prod Res ; 36(18): 4787-4793, 2022 Sep.
Article in English | MEDLINE | ID: mdl-34866508

ABSTRACT

Bioactive compounds extracted from plants such as antimicrobials have attracted the attention of consumers and the food industry. This study aimed to determine the antimicrobial activity and chemical composition of Annona muricata leaf oleoresin obtained by supercritical CO2 extraction. The oleoresin was obtained by supercritical CO2 extraction and the chemical identification by gas chromatography coupled to mass spectrometry. Antimicrobial activity was evaluated by broth microdilution method against 14 foodborne fungi and bacteria. The oleoresin major chemical class was phytosterols (22.7%) and the major compounds were γ-sitosterol (15.7%), α-tocopherol (13.7%), phytol (13.1%), and hexadecanoic acid (11.5%). Minimum inhibitory concentration against bacteria ranged from 0.0025 to 0.010 mg mL-1. The oleoresin had high bactericidal activity against all bacteria, mainly Enterobacter cloacae and Pseudomonas aeruginosa with 0.005 mg mL-1 minimum bactericidal concentration. However, it had low fungicidal activity. The leaf oleoresin of A. muricata has promising applications in food, cosmetic, and pharmaceutical industries.


Subject(s)
Annona , Anti-Infective Agents , Annona/chemistry , Anti-Infective Agents/chemistry , Bacteria , Carbon Dioxide/chemistry , Gas Chromatography-Mass Spectrometry/methods , Plant Extracts/chemistry , Plant Leaves/chemistry
3.
Food Chem ; 259: 270-277, 2018 Sep 01.
Article in English | MEDLINE | ID: mdl-29680054

ABSTRACT

Previous studies have shown that cowpea protein positively interferes with cholesterol metabolism. In this study, we evaluated the ability of the fraction containing peptides of <3 kDa, as well as that of the Gln-Asp-Phe (QDF) peptide, derived from cowpea ß-vignin protein, to inhibit HMG-CoA reductase activity. We established isolation and chromatography procedures to effectively obtain the protein with a purity above 95%. In silico predictions were performed to identify peptide sequences capable of interacting with HMG-CoA reductase. In vitro experiments showed that the fraction containing peptides of <3 kDa displayed inhibition of HMG-CoA reductase activity. The tripeptide QDF inhibits HMG-CoA reductase (IC50 = 12.8 µM) in a dose-dependent manner. Furthermore, in silico studies revealed the binding profile of the QDF peptide and hinted at the molecular interactions that are responsible for its activity. Therefore, this study shows, for the first time, a peptide from cowpea ß-vignin protein that inhibits HMG-CoA reductase and the chemical modifications that should be investigated to evaluate its binding profile.


Subject(s)
Hydroxymethylglutaryl CoA Reductases/metabolism , Hydroxymethylglutaryl-CoA Reductase Inhibitors/metabolism , Peptides/metabolism , Vigna/metabolism , Amino Acid Sequence , Binding Sites , Catalytic Domain , Chromatography, High Pressure Liquid , Chromatography, Reverse-Phase , Humans , Hydroxymethylglutaryl CoA Reductases/chemistry , Hydroxymethylglutaryl-CoA Reductase Inhibitors/chemistry , Molecular Docking Simulation , Peptides/analysis , Peptides/chemistry
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