Abstract
Bromomaleimide-linked bioconjugates are cleavable in mammalian cells.
Highlights
Bromomaleimides have recently been shown to act as small, versatile scaffolds for the controlled assembly of thiolated biomolecules.[1–4] They present three points of chemical attachment, thereby allowing the modular construction of multifunctional bioconjugates
Addition of rhodamine–maleimide was shown to result in efficient quenching of green fluorescent protein (GFP) fluorescence
The efficient quenching of GFP fluorescence allowed us to use the ratio of GFP/rhodamine emission intensities as a quantitative measure of cleavage during subsequent microinjection experiments
Summary
Bromomaleimides have recently been shown to act as small, versatile scaffolds for the controlled assembly of thiolated biomolecules.[1–4] They present three points of chemical attachment, thereby allowing the modular construction of multifunctional bioconjugates. GFP,[6] C48 and C70, were shown to be inaccessible to maleimide functionalisation under our reaction conditions (see Section 4 in the Supporting Information). The folded protein was shown to be GFP-SH to be conjugated to maleimides without the need for resistant to disulfide-mediated dimerisation, allowing reducing agents (see Section 5 in the Supporting Information). S. Caddick Department of Chemistry, University College London the Supporting Information, Section 5.
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