Publication

Adsorbed protein detection by scanning electrochemical microscopy

Abstract

A scanning electrochemical microscopy (SECM) protein detection methodology has been developed based on the tagging of free cysteines and other nucleophiles in proteins and peptides by benzoquinone. The tagged proteins are detected by the mediated reduction of benzoquinone with a redox species produced electrochemically at the SECM tip. After careful optimization, a sensitivity in the low ng mm 2 range was reached for bovine serum albumin. One of the major advantages of the present technique is that the selectivity of the protein tagging can be tuned by changing the pH of the reaction media. Depending on the requirements, cysteine selective or general detection can therefore be achieved with a high sensitivity. As a proof of concept, this technique was applied to the detection of protein spots and to the imaging of human fingerprints and further compared to the actual SECM state-of-art approach.

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Protein purification
Protein purification is a series of processes intended to isolate one or a few proteins from a complex mixture, usually cells, tissues or whole organisms. Protein purification is vital for the specification of the function, structure and interactions of the protein of interest. The purification process may separate the protein and non-protein parts of the mixture, and finally separate the desired protein from all other proteins.
Fusion protein
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