search scholar.google.com.

Papers Published

1. Qi, Y; Amiram, M; Gao, W; McCafferty, DG; Chilkoti, A, Sortase-catalyzed initiator attachment enables high yield growth of a stealth polymer from the C terminus of a protein., Macromolecular rapid communications, vol. 34 no. 15 (August, 2013), pp. 1256-1260 [23836349], [doi] .
   (last updated on 2024/07/16)

   Abstract:
   Conventional methods for synthesizing protein/peptide-polymer conjugates, as a means to improve the pharmacological properties of therapeutic biomolecules, typically have drawbacks including low yield, non-trivial separation of conjugates from reactants, and lack of site- specificity, which results in heterogeneous products with significantly compromised bioactivity. To address these limitations, the use of sortase A from Staphylococcus aureus is demonstrated to site-specifically attach an initiator solely at the C-terminus of green fluorescent protein (GFP), followed by in situ growth of a stealth polymer, poly(oligo(ethylene glycol) methyl ether methacrylate) by atom transfer radical polymerization (ATRP). Sortase-catalyzed initiator attachment proceeds with high specificity and near-complete (≈95%) product conversion. Subsequent in situ ATRP in aqueous buffer produces 1:1 stoichiometric conjugates with >90% yield, low dispersity, and no denaturation of the protein. This approach introduces a simple and useful method for high yield synthesis of protein/peptide-polymer conjugates.