The current invention pertains to stabilized peptoids or peptoid-peptide hybrids. The peptoids or peptoid-peptide hybrids are stabilized by side chain-side to side chain linkages and/or backbone cyclization. The current invention also provides a positional library scanning method for identification of peptoids or peptoid-peptide hybrids having a desired biological activity.

The invention provides methods, compositions, and kits for the characterisation and analysis of proteins. Methods are provided for determining, on a protein, a binding site for a binding partner, the methods comprising: contacting a protein with a plurality of monomers, and polymerising the monomers to create a protein:polymer complex; digesting the protein in the complex to produce a peptide:polymer complex; isolating the peptide:polymer complex; and sequencing the peptide, wherein the peptide corresponds to a binding site for a binding partner.

The invention belongs to the field of chemical analysis and detection, and specifically relates to a pretreatment method for LC-MS detecting metabolomics of Aspergillus flavus. The method includes: culturing a strain of Aspergillus flavus; quenching the Aspergillus flavus; disrupting the cell membrane of Aspergillus flavus, and extracting a metabolome. The invention adopts a cold glycerol buffer solution combined with a rapid filtration method for quenching, and a MeOH/DCM/ACN/EA/HCOOH mixture is used as an metabolome extract, thereby achieving the object of efficiently extracting different polar compounds, and metabolome compound coverage is high; pretreatment of the cell metabolomics of Aspergillus flavus by the method of the invention can ensure the repeatability and stability of the metabolomics analysis method and reduce the false positive of the test results.

The present invention relates to a method for the absolute quantification of naturally processed HLA-restricted cancer peptides, i.e. the determination of the copy number of peptide(s) as presented per cell. The present invention can not only be used for the development of antibody therapies or peptide vaccines, but is also highly valuable for a molecularly defined immuno-monitoring, and useful in the processes of identifying of new peptide antigens for immunotherapeutic strategies, such as respective vaccines, antibody-based therapies or adoptive T-cell transfer approaches in cancer, infectious and/or autoimmune diseases.

Provided are a composition for diagnosing vascular disease including an agent measuring a level of interleukin 12 receptor 2 protein in the blood, and a kit for diagnosing vascular disease including the same. Further, provided is a method for diagnosing vascular disease, the method including the step of measuring a level of interleukin 12 receptor 2 protein in a blood sample separated from an individual suspected of having vascular disease. Furthermore, provided are a composition for preventing or treating vascular disease including an interleukin 12 receptor 2 activity inhibitor, and a method of screening a therapeutic agent for vascular disease, the method including the step of treating smooth muscle cells with a test agent for vascular disease treatment and measuring an expression level of interleukin 12 receptor 2.

Provided is a reagent composition for measuring glycated albumin to diagnose the presence or absence of diabetes and a method of measuring glycated albumin using the same, and more particularly is a reagent composition for measuring glycated albumin, the composition including a dye-encapsulated silica nanoparticle-boronic acid, and to a method of measuring glycated albumin using the same. In the reagent composition for measuring glycated albumin, since a dye is encapsulated in silica nanoparticles, the inherent absorption wavelength of the dye is not affected by pH and the composition has excellent stability even when stored for one month or more.

The present invention relates to methods for assessing binding agent specificity, in particular antibody specificity. The present invention thus provides a method of analysing a mixture of polypeptides comprising the steps of: (i) separating the polypeptides in the mixture into a plurality of fractions; (ii) contacting a first aliquot of two or more of the fractions with a plurality of different binding agents attached to one or more solid supports and detecting the binding of the polypeptides to the binding agents in each fraction; (iii) assessing the amino acid composition of the polypeptides in a second aliquot of said fractions by mass spectrometry; and (iv) correlating the binding results detected in step (ii) and the mass spectrometry results from step (iii) to assess the specificity of the binding agents for a polypeptide of interest.

A method of purification and/or separation of glycopeptides and quantitation of same. The method includes contacting a sample comprising glycopeptides to a hydrophilic enrichment substrate under conditions that permit the glycopeptides to bind to the hydrophilic enrichment substrate. The glycopeptides are eluted from the hydrophilic enrichment substrate with an ammonium formate and acetonitrile (ACN) in water solution to create an enriched glycopeptide sample, which may be subjected to analysis to identify specific glycopeptides.

The presently disclosed subject matter provides methods using mass spectrometry for direct profiling of N-linked glycans from a biological sample. In addition, the embodiments of the present invention also disclose novel methods, known as targeted analyte detection (TAD), for improving the detection limit of MALDI-MS. These methods take advantage of the carrier effect of the added standard analytes, which occurs due to the generic sigmoidal shape of the calibration curve. The functionality of TAD depends on the relative enhancement of sensitivity over the increase of the standard deviation at the analysis of target analytes with spiking in exogenous concentration. At certain ranges of exogenous concentration, the increment in the sensitivity overcomes the standard deviation, resulting in an improved LOD. Theoretically, exogenous concentrations approximately at 1 LODorig would generate the optimum LOD improvement. TAD is a cost-effective LOD improvement method, which is not limited to a certain group of analytes, or detection methods or instruments. It can be applied to enhance the detection of any analyte with different detection methods, provided that the analyte of interest can be extracted or is available in synthetic form.

Methods, devices, and reagents are described for performing assays for hemoglobin Ale, glycated albumin, and other glycated proteins. The methods involve a ratio determination between glycated protein and non-glycated protein. In some applications, the assay utilizes LOCI for signal generation. This invention is directed to assays and corresponding devices and reagents for detection of glycated protein, particularly including glycated hemoglobin. As is generally understood, such detection is useful in the management of blood glucose levels in diabetic patients and for monitoring the status of pre-diabetic individuals.