Maleimide PEG, a subset of polyethylene glycol (PEG), features a maleimide group at one terminal end, serving as an effective handle for streamlined functionalization through thiol–maleimide conjugation and Diels–Alder cycloaddition click reactions.
The expeditious and straightforward reaction between a thiol and a maleimide, leading to the formation of a thiosuccinimide product, has emerged as a preeminent method for site-selective modification of cysteine residues within the realm of bioconjugation technology. Within the pH range of 6.5 to 7.5, the thiol-maleimide reaction demonstrates chemoselectivity for thiols and engenders stable thioether bonds. It is noteworthy that beyond pH 7.5, free primary amines competitively react at the maleimide double bond. PEG Maleimide proves invaluable for bioconjugation and protein labeling endeavors, offering the capability to affix small molecules with PEG chains to proteins, peptides, or surfaces featuring sulfhydryl groups. This versatile application underscores the utility of Maleimide PEG in facilitating precise and controlled modifications in diverse biotechnological contexts.
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