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Carbon dots (CDs) have recently garnered significant attention owing to their excellent luminescence properties, thereby demonstrating a variety of applications in in vitro and in vivo imaging. Understanding the long-term metabolic fate of these agents in a biological environment is the focus of this work. Here we show that the CDs undergo peroxide catalysed degradation in the presence of lipase. Our results indicate that differently charged CD species exhibit unique degradation kinetics upon being subjected to enzyme oxidation. Furthermore, this decomposition correlates with the relative accessibility of the enzymatic molecule. Using multiple physico-chemical characterization studies and molecular modelling, we confirmed the interaction of passivating surface abundant molecules with the enzyme. Finally, we have identified hydroxymethyl furfural as a metabolic by-product of the CDs used here. Our results indicate the possibility and a likely mechanism for complete CD degradation in living systems that can pave the way for a variety of biomedical applications.
This article was published in the following journal.
Materials for photosensitized oxygen activation is extremely important for a suite of photodynamic applications in biomedical, analytical and energy sectors. Carbon-based photosensitizers are attracti...
Nitrogen and phosphorus co-doped carbon dots (N,P-CDs) have been synthesized via hydrothermal method starting from o-phosphorylethanolamine and citric acid. The blue-green fluorescence of the N,P-CDs ...
Drug traversal across the blood-brain barrier has come under increasing scrutiny recently, particularly concerning the treatment of sicknesses, such as brain cancer and Alzheimer's disease. Most thera...
Multicolor, fluorescent self-healing gels were constructed through reacting carbon dots produced from different aldehyde precursors with branched polyethylenimine. The self-healing gels were formed th...
The formation of reactive manganese (Mn) species is emerging as a key regulator of carbon oxidation rates, and thus CO emissions, in soils and sediments. Many subsurface environments are characterized...
This study will test the effectiveness of two different tuberculosis (TB) prevention strategies, DOTS or DOTS-A. DOTS is the current prevention strategy for TB. DOTS-A is an enhanced preve...
Tuberculosis (TB) is the most common opportunistic infection among HIV infected persons living in developing countries. Directly observed treatment, short-course (DOTS) is the internationa...
Most of the guidelines on the treatment of tuberculosis suggest that 6 months treatment is sufficient for extrapulmonary tuberculosis except for bone tuberculosis and tubercular meningitis...
This study is designed as a cluster-randomized trial. The cluster unit is at the community level. Communities will be randomized to 1 of 2 study arms: DOTS+ACF or DOTS. Communities in t...
OBJECTIVES: I. Characterize inheritance patterns of mutations in patients with beta-oxidation disorders.
Enzymes that catalyze the cleavage of a carbon-carbon bond by means other than hydrolysis or oxidation. This subclass contains the DECARBOXYLASES, the ALDEHYDE-LYASES, and the OXO-ACID-LYASES. EC 4.1.
Enzymes of the isomerase class that catalyze the oxidation of one part of a molecule with a corresponding reduction of another part of the same molecule. They include enzymes converting aldoses to ketoses (ALDOSE-KETOSE ISOMERASES), enzymes shifting a carbon-carbon double bond (CARBON-CARBON DOUBLE BOND ISOMERASES), and enzymes transposing S-S bonds (SULFUR-SULFUR BOND ISOMERASES). (From Enzyme Nomenclature, 1992) EC 5.3.
A carbon-carbon double bond isomerase that catalyzes the movement double bond from C3 to C2 of an unsaturated acyl-CoA. The enzyme plays a key role in allowing acyl-CoA substrates to re-enter the beta-oxidation pathway.
An enzyme found primarily in SULFUR-REDUCING BACTERIA where it plays an important role in the anaerobic carbon oxidation pathway.
A light-activated enzyme that catalyzes the oxidation of (S)-malate to OXALOACETATE. It is involved in PYRUVATE metabolism and CARBON fixation.
Enzymes are proteins that catalyze (i.e., increase the rates of) chemical reactions. In enzymatic reactions, the molecules at the beginning of the process, called substrates, are converted into different molecules, called products. Almost all chemical re...
Biological therapy involves the use of living organisms, substances derived from living organisms, or laboratory-produced versions of such substances to treat disease. Some biological therapies for cancer use vaccines or bacteria to stimulate the body&rs...