The present disclosure relates to a method for labeling a radioisotope, a radiolabeling compound, a kit including the same, and a method for labeling a radioisotope, including: providing a diaminophenyl compound represented by Chemical Formula I below and including a biomolecule, a fluorescent dye or a nanoparticle compound bound thereto; and reacting the diaminophenyl compound and a radioisotope-labeled aldehyde compound represented by Chemical Formula II below at room temperature; and a related technology:

##STR00001## in Chemical Formula I, A is CH.sub.2 or O; a is 0 or an integer of 1 to 10; X is CH.sub.2 or CONH; Y is CH.sub.2 or

##STR00002##

and Z is the biomolecule, the fluorescent dye or the nanoparticle compound,

##STR00003## in Chemical Formula II, b is 0 or an integer of 1 to 10; and L is CH.sub.2 or CONH; and Q is or

##STR00004## M, M and M in Q are radioisotopes.

A method for preparing a radiolabeled pharmaceutical. The method comprises passing a mixture that includes a radiolabeled compound through a column that contains an ion exchange resin to retain the radiolabeled compound on the ion exchange resin. At least a portion of the mixture passes through the column without being retained on the ion exchange resin. The method further comprises eluting the radiolabeled compound off the ion exchange resin using an eluting solution (e.g., a sodium chloride solution) to form a radiolabeled pharmaceutical.

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.

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.

Provided herein are bifunctional compounds that bind tau protein and/or promote targeted ubiquitination for the degradation of tau protein. In particular, provided are compounds that can bind tau protein, a protein whose aggregation is implicated in a variety of neurodegenerative disease (e.g., tauopathies), and can promote its degradation by recruiting an E3 ubiquitin ligase (e.g., Cereblon), which can ubiquitinate tau protein, marking it for proteasomal degradation. Also provided are radiolabeled forms of the bifunctional compounds, pharmaceutical compositions comprising the bifunctional compounds, methods of detecting and/or diagnosing neurological disorders, methods of detecting and/or diagnosing pathological aggregation of tau protein (e.g., in the central nervous system), methods of treating and/or preventing neurological disorders, and methods of promoting the degradation of tau protein by E3 ubiquitin ligase activity in a subject by administering a compound or composition described herein.

Provided herein are bifunctional compounds that bind tau protein and/or promote targeted ubiquitination for the degradation of tau protein. In particular, provided are compounds that can bind tau protein, a protein whose aggregation is implicated in a variety of neurodegenerative disease (e.g., tauopathies), and can promote its degradation by recruiting an E3 ubiquitin ligase (e.g., Cereblon), which can ubiquitinate tau protein, marking it for proteasomal degradation. Also provided are radiolabeled forms of the bifunctional compounds, pharmaceutical compositions comprising the bifunctional compounds, methods of detecting and/or diagnosing neurological disorders, methods of detecting and/or diagnosing pathological aggregation of tau protein (e.g., in the central nervous system), methods of treating and/or preventing neurological disorders, and methods of promoting the degradation of tau protein by E3 ubiquitin ligase activity in a subject by administering a compound or composition described herein.

The present disclosure is directed to methods (e.g., in vitro methods) for use of nicotinamide phosphoribosyltransferase (NAMPT) as a biomarker in radiation-induced lung injury (RILI). Provided herein is an in vitro method for the diagnosis, prognosis, and/or monitoring of RILI in a human subject by providing a tissue or plasma sample from the subject and detecting the level of NAMPT therein, wherein a higher level of NAMPT in the tissue or plasma sample from the subject compared to a healthy control or a reference value is indicative for the presence of RILI in the subject. Further provided herein is a method of detecting NAMPT in a human subject by obtaining a biological sample from the subject, detecting the presence of NAMPT in the sample by contacting the sample with a capture agent that specifically binds NAMPT, and detecting binding between NAMPT and the capture agent.

The present disclosure is directed to methods (e.g., in vitro methods) for use of nicotinamide phosphoribosyltransferase (NAMPT) as a biomarker in radiation-induced lung injury (RILI). Provided herein is an in vitro method for the diagnosis, prognosis, and/or monitoring of RILI in a human subject by providing a tissue or plasma sample from the subject and detecting the level of NAMPT therein, wherein a higher level of NAMPT in the tissue or plasma sample from the subject compared to a healthy control or a reference value is indicative for the presence of RILI in the subject. Further provided herein is a method of detecting NAMPT in a human subject by obtaining a biological sample from the subject, detecting the presence of NAMPT in the sample by contacting the sample with a capture agent that specifically binds NAMPT, and detecting binding between NAMPT and the capture agent.

Radiolabeled anti-MET antibodies and METMET bispecific antibodies and their use in immuno-PET imaging are provided herein. Included are methods of detecting the presence of MET proteins in a subject or sample and methods of monitoring efficacy of treatment of a Met expressing tumor.

Methods for producing isotopically-labelled peptides are provided. Aspects of the method include: contacting a sample including a metabolically tagged protein with a cleavable probe to produce a probe-protein conjugate; separating the probe-protein conjugate from the sample; digesting the probe-protein conjugate to produce a probe-peptide conjugate; and cleaving a cleavable linker to release an isotopically labelled peptide. The method may further include: identifying a predetermined isotopic pattern in a mass spectrum; determining an amino acid sequence of the isotopically labelled peptide; and identifying the site of protein glycosylation based on the determined amino acid sequence. Also provided are cleavable probes for practicing the subject methods, described by the Formula: A-L-(M-Z) where A is an affinity tag, L is a cleavable linker, M is an isotopic label and Z is a chemoselective tag capable of cross-linking a metabolically tagged protein. Compositions and kits for practicing the subject methods are also provided.