Potassium Acyltrifluoroborate (KAT) Ligations are Orthogonal to Thiol‐Michael and SPAAC Reactions: Covalent Dual Immobilization of Proteins onto Synthetic PEG Hydrogels
Beschreibung:
<jats:p>The covalent immobilization of peptides, proteins, and other biomolecules to hydrogels provides a biologically mimicking environment for cell and tissue growth. Bioorthogonal chemical reactions can serve as a tool for this, but the paucity of such reactions and mutual incompatibilities limits the number of distinct molecules that can be introduced. We now report that the potassium acyltrifluoroborate (<jats:styled-content style="fixed-case">KAT</jats:styled-content>) amide‐forming ligation is orthogonal to both thiol‐<jats:italic>Michael</jats:italic> and strain promoted azide alkyne cycloadditions (<jats:styled-content style="fixed-case">SPAAC</jats:styled-content>) and the requisite functional groups – <jats:styled-content style="fixed-case">KAT</jats:styled-content>s and hydroxylamines – are stable and compatible to hydrogel formation, protein modification, and post‐assembly immobilization of biomolecules onto hydrogels. In combination these ligations enables stepwise covalent protein immobilization of multiple <jats:styled-content style="fixed-case">BSA</jats:styled-content>‐derivatives onto the hydrogel scaffold regardless of the order of addition.</jats:p>