Abstract:
The present application provides stable peptide-based IDO1 capture agents and methods of use as detection, imaging, diagnostic and therapeutic agents. The application further provides methods of manufacturing IDO1 imaging agents.
Abstract:
Immunoglobulin light chain proteins are used to generate synthetic fibrils in vitro . The fibrils are mixed with immunoglobulin light chain proteins from a biological sample. In either a direct binding assay, competition assay, or dilution-based competition assay, a signal is detected from the mixture. The intensity of the detectable signal relates to the level of binding between the immunoglobulin light chain proteins to the fibrils and can thus be used to identify amyloidogenic immunoglobulin light chain proteins in a biological sample of the subject and to assess amyloidogenic risk to a subject. For example, the signal intensities from the assays can be used in a comparison to one or more threshold (control) values derived from samples of known light chain types or in the absence of light chains. The comparisons permit identification of amyloidogenic proteins, assessment of amyloidogenic risk, and categorization of the subject into an appropriate "at risk" group.
Abstract:
Macromolecular conjugates for visualization and separation of proteins and cells The present invention descripbes macromolecular water-soluble conjugates based on synthetic copolymers to which at least one affinity tag, at least one imaging probe and at least one targeting ligand are bound via covalent bonds. The macromolecular conjugate may be used in identification, visualization, quantification or isolation of proteins and/or cells both in vitro and in vivo. HPMA copolymer, i.e.poly(HPMA-co-Ma-β-Ala-TT), copolymer prepared by conventional solution radical polymerization or controlled radical copolymerization (e.g. RAFT copolymerization, reversible addition-fragmentation chain-transfer) of N-(2- hydroxypropyl)methacrylamide (HPMA) and 3-(3-methakrylamidopropanoyl)thiazolidine-2-thione (Ma-P-Ala-TT) can be preferably used as the basic copolymer.
Abstract:
Provided herein are methods, compositions and kits for use in the site-specific labeling of glycoproteins comprising a combination of enzyme-mediated incorporation of modified sugars comprising a chemical handle and cycloaddition chemistry with a labeling molecule comprising a reactive group, a metal ion chelator, and/or a fluorophore.
Abstract:
Es wird die Verwendung eines Peptids (1) zur Herstellung eines Agens zur Detektion eines krankhaften Gewebes (18) beschrieben. Die Aminosäuresequenz des Peptids (1) stammt dabei von der Aminosäuresequenz eines Proteins ab, das von dem krankhaften Gewebe (18) gebildet wird, und das Peptid (1) bindet an einen humanen Leukozytenantigen (HLA) Komplex (4), der ebenfalls von dem krankhaften Gewebe (18) gebildet wird. Des Weiteren weist das Peptid (1) ein 11 C-Kohlenstoffatom auf. Ferner wird ein Radiopharmakon zur Lokalisation eines krankhaften Gewebes (18) beschrieben, das ein solches Peptid (1) umfasst.
Abstract:
The present invention features noninvasive methods for diagnosing IgA or IgM kidney disorders, such as IgA nephropathy, Henoch-Schdnlein purpura, and IgM nephropathy, in a mammal. The invention also features compositions and kits useful in diagnosing these disorders.
Abstract:
The invention provides a method for identifying a candidate imaging probe, the method comprising: a) contacting a first library of candidate compounds with a target biomacromolecule, b) identifying a first member from the first library exhibiting affinity for the first binding site; c) contacting the first member identified from the first library affinity for the first binding site with the target biomacromolecule; d) contacting a second library of candidate compounds with the first member and the target biomacromolecule, e) reacting the complementary first functional group with the second functional group via a biomacromolecule induced click chemistry reaction to form the candidate imaging probe; f) isolating and identifying the candidate imaging probe; g) preparing the candidate imaging probe by chemical synthesis; and h) for imaging applications, converting the candidate imaging probe into an imaging probe.
Abstract:
The invention provides a method for identifying a candidate imaging probe, the method comprising: a) contacting a first library of candidate compounds with a target biomacromolecule, b) identifying a first member from the first library exhibiting affinity for the first binding site; c) contacting the first member identified from the first library affinity for the first binding site with the target biomacromolecule; d) contacting a second library of candidate compounds with the first member and the target biomacromolecule, e) reacting the complementary first functional group with the second functional group via a biomacromolecule induced click chemistry reaction to form the candidate imaging probe; f) isolating and identifying the candidate imaging probe; g) preparing the candidate imaging probe by chemical synthesis; and h) for imaging applications, converting the candidate imaging probe into an imaging probe.
Abstract:
Mit dem erfindungsgemäßen Verfahren zur selektiven Markierung von Peptiden wird insbesondere der Schritt der selektiven radioaktiven Markierung einzelner Aminogruppen der Peptide in Lösung ermöglicht. Peptide können dabei unabhängig ihrer Sequenz bereits ab dem Mikrogramm (µg)-Maßstab selektiv radioaktive markiert werden. Dazu wird bei der Peptidsynthese an mindestens einer später zu markierenden Position ein Aminosäurebaustein eingebaut, der eine Aminogruppe trägt, die durch eine Gruppe geschützt wird, die sich funktionell von den Schutzgruppen an den nicht zu markierenden Aminogruppen unterscheidet. Im Anschluss an die Peptidsynthese wird die Schutzgruppe an der zu markierenden Position selektiv entfernt and das Peptid vom Trägermaterial gelöst. In das so erhaltene selektiv-entschützte Peptid wird in Lösung an der zu markierenden Position über aminoreaktive Substanzen eine Markierung eingeführt. Die Schutzgruppen an den nicht zu markierenden Aminogruppen werden nach der Markierung in einfacher Weise, vorzugsweise durch UV-Licht abgespalten, und das so erhaltene selektiv markierte Peptid in bekannter Weise gereinigt.
Abstract:
Salt sensitivity is measured as a function of the urinary 25-OHD binding activity, which may be evaluated by measuring 25-hydroxyvitamin D binding activity using radiolabeled 25-hydroxyvitamin D3. High binding activity is indicative of salt sensitivity and is an important predictor for development of salt-sensitivity related hypertension.