The proteome is a highly complex mixture of diverse proteins and peptides in varying concentrations and conditions. The qualitative and quantitative analysis of this mixture is a challenging task even with today's advanced separation and analysis capabilities.

The unique features of Capture Compound™ Mass Spectrometry (CCMS) are based on the multifunctionality of caprotec's proprietary Capture Compound molecules.

Capture Compounds allow a reversible affinity interaction between proteins through a selectivity function; a reactivity function forms a covalent bond with interacting proteins and a pull out function allows isolating the captured proteins directly from cell lysates.

The CCMS process can be characterized as a homogeneous reverse High-Throughput Screening: The proteome is treated as a library and screened for the affinity of individual proteins which interact with the selectivity group of the small Capture Compound.

These compounds target specific enzyme families through affinities to a defined small molecule. Capture Compounds are proprietary, synthetic molecules, designed to include a selectivity function (e.g. an enzyme substrate/inhibitor, cofactor or, drug candidate), a reactivity function (to covalently bind the protein target), and a sorting function (to pull the Capture Compound-Protein-complex directly out of cell lysates).

 

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Capture Compounds™ enable an efficient complexity reduction of the proteome to a subset of proteins based on their affinity to the selectivity group. Thus, CCMS allows discovering, isolating and profiling members of functional protein families within biological samples.

The CCMS method is highly versatile, since virtually any small molecule can act as a selectivity function within a Capture Compound™ and protein samples from virtually any source can be investigated. A typical CCMS experiment can be divided into three phases: 1) Sample preparation, 2) Covalent cross-linking and 3) Protein isolation and identification.