Positron emissionPositron emission, beta plus decay, or β+ decay is a subtype of radioactive decay called beta decay, in which a proton inside a radionuclide nucleus is converted into a neutron while releasing a positron and an electron neutrino (νe). Positron emission is mediated by the weak force. The positron is a type of beta particle (β+), the other beta particle being the electron (β−) emitted from the β− decay of a nucleus.
Molecular imagingMolecular imaging is a field of medical imaging that focuses on imaging molecules of medical interest within living patients. This is in contrast to conventional methods for obtaining molecular information from preserved tissue samples, such as histology. Molecules of interest may be either ones produced naturally by the body, or synthetic molecules produced in a laboratory and injected into a patient by a doctor. The most common example of molecular imaging used clinically today is to inject a contrast agent (e.
Oxygen-18Oxygen-18 (18O, Ω) is a natural, stable isotope of oxygen and one of the environmental isotopes. 18O is an important precursor for the production of fluorodeoxyglucose (FDG) used in positron emission tomography (PET). Generally, in the radiopharmaceutical industry, enriched water (H218O) is bombarded with hydrogen ions in either a cyclotron or linear accelerator, producing fluorine-18. This is then synthesized into FDG and injected into a patient. It can also be used to make an extremely heavy version of water when combined with tritium (hydrogen-3): 3H218O or T218O.
Carbon–fluorine bondThe carbon–fluorine bond is a polar covalent bond between carbon and fluorine that is a component of all organofluorine compounds. It is one of the strongest single bonds in chemistry (after the B–F single bond, Si–F single bond, and H–F single bond), and relatively short, due to its partial ionic character. The bond also strengthens and shortens as more fluorines are added to the same carbon on a chemical compound. As such, fluoroalkanes like tetrafluoromethane (carbon tetrafluoride) are some of the most unreactive organic compounds.
ProteinopathyIn medicine, proteinopathy ([pref. protein]; -pathy [suff. disease]; proteinopathies pl.; proteinopathic adj), or proteopathy, protein conformational disorder, or protein misfolding disease, is a class of diseases in which certain proteins become structurally abnormal, and thereby disrupt the function of cells, tissues and organs of the body. Often the proteins fail to fold into their normal configuration; in this misfolded state, the proteins can become toxic in some way (a toxic gain-of-function) or they can lose their normal function.
Organofluorine chemistryOrganofluorine chemistry describes the chemistry of organofluorine compounds, organic compounds that contain a carbon–fluorine bond. Organofluorine compounds find diverse applications ranging from oil and water repellents to pharmaceuticals, refrigerants, and reagents in catalysis. In addition to these applications, some organofluorine compounds are pollutants because of their contributions to ozone depletion, global warming, bioaccumulation, and toxicity.
Ligand (biochemistry)In biochemistry and pharmacology, a ligand is a substance that forms a complex with a biomolecule to serve a biological purpose. The etymology stems from Latin ligare, which means 'to bind'. In protein-ligand binding, the ligand is usually a molecule which produces a signal by binding to a site on a target protein. The binding typically results in a change of conformational isomerism (conformation) of the target protein. In DNA-ligand binding studies, the ligand can be a small molecule, ion, or protein which binds to the DNA double helix.
Binding siteIn biochemistry and molecular biology, a binding site is a region on a macromolecule such as a protein that binds to another molecule with specificity. The binding partner of the macromolecule is often referred to as a ligand. Ligands may include other proteins (resulting in a protein-protein interaction), enzyme substrates, second messengers, hormones, or allosteric modulators. The binding event is often, but not always, accompanied by a conformational change that alters the protein's function.
PeptidePeptides are short chains of amino acids linked by peptide bonds. A polypeptide is a longer, continuous, unbranched peptide chain. Polypeptides which have a molecular mass of 10,000 Da or more are called proteins. Chains of fewer than twenty amino acids are called oligopeptides, and include dipeptides, tripeptides, and tetrapeptides. Peptides fall under the broad chemical classes of biological polymers and oligomers, alongside nucleic acids, oligosaccharides, polysaccharides, and others.
ElastographyElastography is any of a class of medical imaging modalities that map the elastic properties and stiffness of soft tissue. The main idea is that whether the tissue is hard or soft will give diagnostic information about the presence or status of disease. For example, cancerous tumours will often be harder than the surrounding tissue, and diseased livers are stiffer than healthy ones. The most prominent techniques use ultrasound or magnetic resonance imaging (MRI) to make both the stiffness map and an anatomical image for comparison.
