A5084024321- Redox biology and oxidative stress
- Advanced Glycation End Products research
- Protein Hydrolysis and Bioactive Peptides
- Biochemical effects in animals
- Photodynamic Therapy Research Studies
- Free Radicals and Antioxidants
- Electron Spin Resonance Studies
- Photosynthetic Processes and Mechanisms
- Neonatal Health and Biochemistry
- Nitric Oxide and Endothelin Effects
- Phytochemicals and Antioxidant Activities
- Antioxidant Activity and Oxidative Stress
- Metabolism and Genetic Disorders
- Meat and Animal Product Quality
- Mitochondrial Function and Pathology
- Biomedical Research and Pathophysiology
- bioluminescence and chemiluminescence research
- Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Proteins in Food Systems
- Food Allergy and Anaphylaxis Research
- Molecular Biology Techniques and Applications
- Heme Oxygenase-1 and Carbon Monoxide
- Coenzyme Q10 studies and effects
- Hemoglobin structure and function
- Enzyme Structure and Function
Pontificia Universidad Católica de Chile
2015-2025
University of Copenhagen
2017-2024
Universidad de Santiago de Chile
2019-2020
Rede de Química e Tecnologia
2015-2016
When AAPH is employed as a free radical source, at low concentrations of free, peptide and protein Trp residues, the oxidation mostly induced by alkoxyl radicals. However, high concentrations, both peroxyl radicals are involved.
The pentose phosphate pathway (PPP) is a key metabolic pathway. oxidative phase of this process involves three reactions catalyzed by glucose-6-phosphate dehydrogenase (G6PDH), 6-phosphogluconolactonase (6PGL) and 6-phosphogluconate (6PGDH) enzymes. first third steps (catalyzed G6PDH 6PGDH, respectively) are responsible for generating reduced nicotinamide adenine dinucleotide (NAPDH), cofactor maintaining the reducing power cells detoxification both endogenous exogenous oxidants...
We demonstrate from kinetic studies that under the experimental conditions proposed for ORAC protocol, values do not correlate with capacity of antioxidants to trap peroxyl radicals (ROO˙), suggesting a dominant role alkoxyl (RO˙) in assay.
Photo-oxidation of casein proteins is commonplace during milk processing and storage. A major consequence such light exposure protein cross-linking aggregation. Although caseins are key components, the nature cross-links mechanisms involved poorly characterized, with most previous work having been focused on detecting quantifying di-tyrosine formed dimerization two tyrosine-derived phenoxyl radicals. However, this only one a large number possible that might be formed. In study, we have...
Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a key cellular enzyme, with major roles in both glycolysis, and 'moonlighting' activities the nucleus (uracil DNA glycosylase activity, nuclear protein nitrosylation), as regulator of mRNA stability, transferrin receptor, an antimicrobial agent. These are dependent, at least part, on integrity active site Cys residue, second neighboring Cys. residues differentially sensitive to oxidation, determine its catalytic activity redox signaling...
Biological systems are heterogeneous and crowded environments. Such packed milieus expected to modulate reactions both inside outside the cell, including protein oxidation. In this work, we explored effect of macromolecular crowding on rate extent oxidation Trp Tyr, in free amino acids, peptides proteins. These species were chosen as they readily oxidized contribute damage propagation. Dextran was employed an inert agent, polymer decreases fraction volume available other (macro)molecules....
The co-existence of proteins, lipids and riboflavin (RF) in milk together with the harsh conditions encountered during processing (e.g. high temperatures, light exposure) results oxidative damage. Proteins represent ~30 % dry mass milk, caseins accounting for ~80 (28 g L−1). Due to their abundance amphiphilic nature, are targets both hydrophilic lipophilic oxidants. Although key components, highly abundant, most previous work has employed non-biological dilute solutions. In this we have...
Dityrosine and ditryptophan bonds have been implied in protein crosslinking. This is associated with oxidative stress conditions including those involved neurodegenerative pathologies age-related processes. Formation of dityrosine derives from radical-radical reactions involving Tyr˙ Trp˙ radicals. However, cross leading to Tyr-Trp crosslinks their biological consequences less explored. In the present work we hypothesized that exposure free Tyr Trp a high concentration carbonate anion...