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1.
Environ Sci Pollut Res Int ; 31(10): 14845-14857, 2024 Feb.
Article in English | MEDLINE | ID: mdl-38285256

ABSTRACT

The global consumption of antibiotics leads to their possible occurrence in the environment. In this context, nature-based solutions (NBS) can be used to sustainably manage and restore natural and modified ecosystems. In this work, we studied the efficiency of the NBS free-water surface wetlands (FWSWs) using Eichhornia crassipes in microcosm for enrofloxacin removal. We also explored the behavior of enrofloxacin in the system, its accumulation and distribution in plant tissues, the detoxification mechanisms, and the possible effects on plant growth. Enrofloxacin was initially taken up by E. crassipes (first 100 h). Notably, it accumulated in the sediment at the end of the experimental time. Removal rates above 94% were obtained in systems with sediment and sediment + E. crassipes. In addition, enrofloxacin was found in leaves, petioles, and roots (8.8-23.6 µg, 11-78.3 µg, and 10.2-70.7 µg, respectively). Furthermore, enrofloxacin, the main degradation product (ciprofloxacin), and other degradation products were quantified in the tissues and chlorosis was observed on days 5 and 9. Finally, the degradation products of enrofloxacin were analyzed, and four possible metabolic pathways of enrofloxacin in E. crassipes were described.


Subject(s)
Eichhornia , Water Pollutants, Chemical , Wetlands , Ecosystem , Enrofloxacin , Water Pollutants, Chemical/analysis , Biodegradation, Environmental
2.
ChemMedChem ; 18(12): e202200691, 2023 06 15.
Article in English | MEDLINE | ID: mdl-36995341

ABSTRACT

The multifactorial nature of Alzheimer's disease (AD) is now widely recognized, which has increased the interest in compounds that can address more than one AD-associated targets. Herein, we report the inhibitory activity on the human cholinesterases (acetylcholinesterase, hAChE and butyrylcholinesterase, hBChE) and on the AChE-induced ß-amyloid peptide (Aß) aggregation by a series of peptide derivatives designed by mutating aliphatic residues for aromatic ones. We identified peptide W3 (LGWVSKGKLL-NH2 ) as an interesting scaffold for the development of new anti-AD multitarget-directed drugs. It showed the lowest IC50 value against hAChE reported for a peptide (0.99±0.02 µM) and inhibited 94.2 %±1.2 of AChE-induced Aß aggregation at 10 µM. Furthermore, it inhibited hBChE (IC50 , 15.44±0.91 µM), showed no in vivo toxicity in brine shrimp and had shown moderated radical scavenging and Fe2+ chelating capabilities in previous studies. The results are in line with multiple reports showing the utility of the indole moiety for the development of cholinesterase inhibitors.


Subject(s)
Alzheimer Disease , Amyloid beta-Peptides , Humans , Acetylcholinesterase/metabolism , Butyrylcholinesterase/metabolism , Structure-Activity Relationship , Cholinesterase Inhibitors/pharmacology , Cholinesterase Inhibitors/chemistry , Alzheimer Disease/drug therapy
3.
Vet Immunol Immunopathol ; 251: 110460, 2022 Sep.
Article in English | MEDLINE | ID: mdl-35901545

ABSTRACT

Low-cost adjuvants are urgently needed for the development of veterinary vaccines able to trigger strong immune responses. In this work, we describe a method to obtain a low-cost cage-like particles (ISCOMATRIX-like) adjuvant useful to formulate veterinary vaccines candidates. The main components to form the particles are lipids and saponins, which were obtained from egg yolk by ethanolic extraction and by dialyzing a non-refined saponins extract, respectively. Lipids were fully characterized by thin layer chromatography (TLC) and gas-chromatography (GC) and enzymatic methods, and saponins were characterized by TLC, HPLC and MALDI-TOF. Cage-like particles were prepared with these components or with commercial inputs. Both particles and the traditional Alum used in veterinary vaccines were compared by immunizing mice with Ovalbumin (OVA) formulated with these adjuvants and assessing IgG1, IgG2a anti OVA antibodies and specific Delayed-type Hypersensitivity (DTH). In the yolk extract, a mixture of phospholipids, cholesterol and minor components of the extract (e.g. lyso-phospholipids) with suitable proportions to generate cage-like particles was obtained. Also, semi-purified saponins with similar features to those of the QuilA® were obtained. Cage-like particles prepared with these components have 40-50 nm and triggers similar levels of Anti-OVA IgG1 and DTH than with commercial inputs but higher specific-IgG2a. Both adjuvants largely increased the levels of IgG1, IgG2a and DTH in relation to the formulation with Alum. The methods described to extract lipids from egg yolk and saponins from non-refined extract allowed us to obtain an inexpensive and highly effective adjuvant.


Subject(s)
Saponins , Vaccines , Adjuvants, Immunologic/chemistry , Animals , Immunoglobulin G , Mice , Ovalbumin
4.
Chem Biodivers ; 16(1): e1800472, 2019 Jan.
Article in English | MEDLINE | ID: mdl-30412651

ABSTRACT

Alzheimer's disease (AD) is the most common cause of dementia, characterized by loss of selective neuronal and normal brain functions. Every year, ten million new cases are diagnosed worldwide. AD is a complex disease associated with all kind of different pathways, making their simultaneous modulation necessary. Nowadays anti-AD treatments are focused on enzymatic inhibitors. The study of the amphibians' skin had acquired great importance in the fields of biology and human health and represents an attractive and novel source for natural compounds with high potential in the development of new drugs. The present work exhibits the power of amphibian skins as a source of bioactive compounds. Herein we report the activity of extracts of two species from Hylidae family (H. cordobae and P. minuta) as reversible inhibitors of acetylcholinesterase and butyrylcholinesterase enzymes. Furthermore, the extracts inhibit MAO-B enzyme and showed antioxidant activities, acting on four important pathways of AD.


Subject(s)
Alzheimer Disease/metabolism , Antioxidants/isolation & purification , Antioxidants/pharmacology , Cholinesterase Inhibitors/isolation & purification , Cholinesterase Inhibitors/pharmacology , Monoamine Oxidase Inhibitors/isolation & purification , Monoamine Oxidase Inhibitors/pharmacology , Skin/chemistry , Acetylcholinesterase/drug effects , Acetylcholinesterase/metabolism , Alzheimer Disease/enzymology , Animals , Antioxidants/administration & dosage , Anura/classification , Butyrylcholinesterase/drug effects , Butyrylcholinesterase/metabolism , CHO Cells , Cholinesterase Inhibitors/administration & dosage , Chromatography, High Pressure Liquid , Chromatography, Reverse-Phase , Chromatography, Thin Layer , Cricetulus , Dose-Response Relationship, Drug , Electrophoresis, Polyacrylamide Gel , Erythrocytes/drug effects , Erythrocytes/enzymology , Humans , Monoamine Oxidase/drug effects , Monoamine Oxidase/metabolism , Monoamine Oxidase Inhibitors/administration & dosage , Species Specificity , Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization , Spectrophotometry, Ultraviolet
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