ABSTRACT
An investigation of reversible protein conjugation and deconjugation is presented. Despite numerous available protein conjugation methods, there has been limited documentation of achieving protein conjugation in a controlled and reversible manner. This report introduces a protocol that enables protein modification in a multicomponent fashion under aqueous buffer and mild conditions. A readily available mercaptobenzaldehyde derivative can modify the primary amine of peptides and proteins with a distinctive [3.3.1] scaffold. This modification can be reversed under mild conditions in a controlled fashion, restoring the original protein motif. The effectiveness of this approach has been demonstrated in the modification and quantifiable regeneration of insulin protein.
