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Overview
ProteinPrint™

 

Molecular Imprinting

 

Selection

Self-Assembly

Polymerization

Extraction

Molecular imprinting is a process by which functional monomers are allowed to self-assemble around a template molecule and subsequently crosslinked into place. Under defined conditions, the template molecule can be removed, leaving behind a cavity complementary in shape and functionality, which will bind molecules identical to the template. The imprint functions like a lock that is only compatible with the correct key.

Molecular imprinting was used as early as the 1930's by MV Polyakov to selectively capture various additives in a silica matrix. In the 1940's Linus Pauling hypothesized that a process similar to molecular imprinting could be responsible for the selectivity of antibodies to their respective antigens. The theory was supported by experiments done by his graduate student, Frank Dickey, who demonstrated imprinting and specific adsorption of several different dyes in silica. We now know that antibodies are produced by clonal-selection, but the idea of a pliable antibody taking shape in response to a foreign antigen was intriguing. Imprinting in silica gained some popularity over the next 15 years, but did not really catch on due to the instability of the silica matrix and limitations in the diversity of compatible templates molecules. The concept of molecular imprinting was revived in the 1970's when Günter Wulff discovered that highly crosslinked organic polymers could also be used to make molecular imprints with high specificity. In more recent years, imprinted polymers have been used to capture everything from steroids to TNT. Today, Aspira's innovative methods improve on these 70 years of research to enable the capture of large and fragile proteins.

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