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New reagents for protein modification
Reagents that can selectively modify individual amino acids are of widespread use in the study and manipulation of proteins. They enable; the mimicking of post-translational modification; the installation of tags such as fluorophores for protein visualisation or biotin for immobilisation and purification; the conjugation of two or more biomolecules; and efficient access to modified proteins as potential therapeutics. Cysteine is often the most nucleophilic residue in a protein, and as such is generally regarded the easiest to modify in a selective manner. One of the most widely used reactive motifs for cysteine modification are maleimides. Notably however maleimides react irreversibly and thus cannot be cleaved in subsequent steps to regenerate the free cysteine. Such reversibility is extremely useful as it allows the modification to be temporary. We are developing a new class of maleimide reagents for the modification of cysteine. We have reported on the use of bromomaleimide which reacts efficiently with cysteine to give thiomaleimide 1. We found that bromomaleimide is even more reactive to cysteine than maleimide itself, and it is highly selective for thiols over amines. Treatment of thiomaleimide 1 with base leads to elimination to afford dehydroalanine, a useful amino-acid which can be further derivatized. We have also shown that bromomaleimides can carry out highly selective and reversible modification of cysteine residues in proteins (collaboration with Prof Steve Caddick). Within this work we demonstrated that bromomaleimides contain three points of attachment for bioconjugation by the construction of a glycoprotein mimic 3 and by the bridging of somatostatin, to produce a fluorescent somatostatin analogue.
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