The invention concerns the field of detecting and quantifying misfolded proteins/peptides. In particular the detection and quantification of misfolded proteins/peptides in body fluids, on cell surfaces of humans and mammals, the detection of misfolded proteins/peptides in reagents to be tested for scientific research and/or diagnostic use and in pharmaceutical medication or their additives and it concerns as well the removal of misfolded proteins/peptides from reagents to be tested for scientific research and/or for diagnostic purposes and from pharmaceutical medication or their additives. Furthermore the invention includes substances to identify and methods to detect bio-films, a method to examine hemocompatibility of materials and a method to optimize therapeutical products, and to provide reagents microorganisms to charge with for more reliable diagnostics and quality control of biopharmaceuticals and identification substances for the screening for preliminary stages of amyloids that can be used for technical purposes.

The invention relates to kits and components thereof used in the conduct of solid-phase binding assays.

A method for determining past exposure to chemical agents or heavy metals may include coating a capture material with a capture reagent. The capture reagent may be selected based on an ability of the capture reagent to bind with a target antibody, and the target antibody may be an indicator associated with a particular chemical agent or heavy metal. The method may further include interrogating a clinical sample associated with an individual by forming a mixture of the capture material and the clinical sample, and determining an exposure status of the individual to the particular chemical agent or heavy metal based on whether the capture material demonstrates capture of the indicator.

Described herein are methods and devices for diagnosing chronic fatigue syndrome using peptide arrays, and providing a prognosis to patients.

The invention relates to a method for identifying and quantifying a polypeptide from a library of polypeptides. The method comprises the steps of: 1providing a polypeptide library and a detection tag library, 2generating a nested library comprising the polypeptides and the detection tags, 3sequencing the nested library, 4selecting a member of the nested library in one or several selection steps that are independent of a physical genotype-phenotype linkage, 5isolating the detection tag from the selected polypeptide, 6identifying and quantifying the detection tag by mass spectrometry, 7obtaining the sequence of the selected polypeptide. The invention also relates to a collection of polypeptides, a collection of detection tags, and a collection of plasmid vectors.

The invention provides arrays of compound for use in profiling samples. The arrays include compounds bind to components of the samples at relatively low affinities. The avidity of compounds binding to components of the samples can be increased by forming arrays such that multivalent components of the samples (e.g., antibodies or cells) can bind to more than one molecule of a compound at the same time. When a sample is applied to an array under such conditions, the compounds of the array bind to component(s) of the sample with significantly different avidities generating a profile characteristic of the sample.

The present invention provides assays and assay systems for use in spatially encoded biological assays. The invention provides an assay system comprising an assay capable of high levels of multiplexing where reagents are provided to a biological sample in defined spatial patterns; instrumentation capable of controlled delivery of reagents according to the spatial patterns; and a decoding scheme providing a readout that is digital in nature.

The present invention provides assays and assay systems for use in spatially encoded biological assays. The invention provides an assay system comprising an assay capable of high levels of multiplexing where reagents are provided to a biological sample in defined spatial patterns; instrumentation capable of controlled delivery of reagents according to the spatial patterns; and a decoding scheme providing a readout that is digital in nature.

A method of analyzing protein-protein interactions includes binding the first proteins to the substrate where the first proteins are tagged with the first markers which bind specifically to the biomolecules immobilized on the substrate or the first proteins bind specifically to the biomolecules immobilized on the substrate; incubating the substrate bound first proteins with cell lysate containing the second proteins which are tagged with second markers; analyzing the interactions between the first proteins and the second proteins in the cell lysate, and obtaining the first analytic value representing the kinetic picture of the interactions; incubating the substrate bound first proteins with cell lysate mixture of a cell lysate consisting of the second markers-tagged second proteins and another cell lysate comprising other proteins including unlabelled second proteins and obtaining the second analytic value; comparing and analyzing the first and the second analytic values.

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.