The present invention provides a reporter for a protein fragment complementation assay characterized in that the reporter is a fused protein comprising a first fragment, a second fragment and a protein kinase sequence section, wherein the first fragment and the second fragment are derived from different sections of the same split protein, and wherein the protein kinase sequence section intervenes between the first fragment and the second fragment and wherein the kinase sequence section comprises a kinase domain sequence and one or more regulatory sequence(s). Further the invention provides polynucleotides and cells encoding for the reporter as well as methods of conducting a protein fragment complementation assay with the reporter according to the invention.

This invention relates to peptide microarrays, methods of generating peptide microarrays, and methods of identifying peptide binders using microarrays. More specifically, this invention relates to peptide microarrays, methods of generating peptide microarrays, and methods of identifying peptide binders using microarrays wherein the microarrays comprise cyclic peptides. The invention also relates to methods and compositions for detecting the formation of cyclized peptides from linear peptides on a microarray by contacting the microarray with a detectable protein. The cyclized peptides include tags that are activated upon cyclization, facilitating the detection of successful cyclization reactions. In additional aspects, the invention relates to developing fragmented peptide tags that, upon cyclization, bind to detectable proteins. Additionally, the invention relates to methods of generating linear and cyclic peptides subarrays on a microarray.

Disclosed are methods for identifying a nucleic acid (e.g., RNA, DNA, etc.) motif which interacts with a ligand. The method includes providing a plurality of ligands immobilized on a support, wherein each particular ligand is immobilized at a discrete location on the support; contacting the plurality of immobilized ligands with a nucleic acid motif library under conditions effective for one or more members of the nucleic acid motif library to bind with the immobilized ligands; and identifying members of the nucleic acid motif library that are bound to a particular immobilized ligand. Also disclosed are methods for selecting, from a plurality of candidate ligands, one or more ligands that have increased likelihood of binding to a nucleic acid molecule comprising a particular nucleic acid motif, as well as methods for identifying a nucleic acid which interacts with a ligand.

This invention relates generally to identifying peptide sequences involved in antibody binding to any protein for synthesis of vaccine treatments. This novel method allows for a more manageable vaccine peptide discovery and specific generation of unique immunogenic peptides from self-tumor associated proteins and/or foreign proteins from infectious organisms for specific and/or enhanced expression only in the presence of the antibody.

The present invention provides for methods of identifying peptoid mimetics that will mimic B cell epitopes when delivered as vaccine compositions. One aspects of the invention is the use of monoclonal antibody that is broadly protective to select the mimetics, thereby identifying an epitope from a pathogen or other disease-causing agent that will be common among most or all variants of that pathogen or agent.

The present invention relates generally methods and kits for detecting binding interactions, in particular protein-protein interactions, and particularly to high throughput methods for labelling, analysing, detecting and measuring protein-protein interactions.

Contemplated test kits and methods for food sensitivity are based on rational-based selection of food preparations with established discriminatory p-value. Particularly preferred kits include those with a minimum number of food preparations that have an average discriminatory p-value of ≦0.07 as determined by their raw p-value or an average discriminatory p-value of ≦0.10 as determined by FDR multiplicity adjusted p-value. In further contemplated aspects, compositions and methods for food sensitivity are also stratified by gender to further enhance predictive value.

Triazabutadiene molecules as cleavable cross-linkers adapted to cross-link components with dick chemistry, e.g., clickable triazabutadienes. For example, in some embodiments, the triazabutadienes feature alkyne handles attached to the imidazole portion or the aryl portion of the triazabutadienes, wherein the alkyne handles can link to azide handles (e.g., azide handles disposed on other components) via dick chemistry. Also described are methods of producing said clickable triazabutadienes and methods of use of said clickable triazabutadienes. The present invention also features methods of cleaving said clickable triazabutadienes, e.g., for liberating the diazonium species for further chemical reactions.

The present disclosure an ELISA-based assay that uses a glycosylated polypeptide fragment derived from the SARS-CoV-2 spike protein (Covid-19) receptor binding domain (S1RBD) that has affinity for the extracellular domain of Angiotensin Converting Enzyme 2 (ACE2). The S1RBD polypeptide is generated by expression of an encoding nucleic acid by a human cell expression system resulting in glycosylation of the expressed spike receptor binding domain (S1RBD) protein at least at the N343 N-glycosylation site thereof, and which surprisingly and significantly increases the affinity of the S1RBD for ACE2, provides a significant increase in the sensitivity of the assay compared to other known assays.

A peptide that binds specifically to neuropilin-1 (NRP1) without binding to neuropilin-2 (NRP2) is provided. A fusion protein, a fusion antibody, small-molecule drug, a nanoparticle, or a liposome, which comprises the peptide, and a pharmaceutical composition for treating or preventing cancer or angiogenesis-related diseases, and a composition for diagnosing cancer or angiogenesis-related diseases are provided. A polynucleotide encoding the peptide that binds specifically to NRP1 and a method for screening the peptide that binds specifically to NRP1 are provided. An antibody heavy-chain constant region Fc-fused peptide binding specifically to NRP1 has the property of binding specifically to NRP1, and thus when it is administered in vivo, it accumulates selectively in tumor tissue, and widens the intercellular space between tumor-associated endothelial cells to promote its extravasation and increases its tumor tissue penetration.