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Construction of Polymer–Protein Bioconjugates with Varying Chain Topologies: Polymer Molecular Weight and Steric Hindrance Effects
Author(s) -
Wan Xuejuan,
Zhang Guoying,
Ge Zhishen,
Narain Ravin,
Liu Shiyong
Publication year - 2011
Publication title -
chemistry – an asian journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.18
H-Index - 106
eISSN - 1861-471X
pISSN - 1861-4728
DOI - 10.1002/asia.201100489
Subject(s) - polymer , copolymer , avidin , biotinylation , polymer chemistry , steric effects , side chain , moiety , monomer , streptavidin , polymerization , molecular recognition , chemistry , materials science , atom transfer radical polymerization , biotin , molecule , organic chemistry , biochemistry
We report on the fabrication of well‐defined polymer–protein bioconjugates with varying chain architectures, including star polymers, star block copolymers , and heteroarm star copolymers through the specific noncovalent interaction between avidin and biotinylated synthetic polymer precursors. Homopolymer and diblock precursors site‐specifically labeled with a single biotin moiety at the chain terminal, chain middle, or diblock junction point were synthesized by a combination of atom‐transfer radical polymerization (ATRP) and click reactions. By taking advantage of molecular recognition between avidin and biotin moieties, supramolecular star polymers, star block copolymers , and heteroarm star copolymers were successfully fabricated. This specific binding process was also assessed by using the diffraction optic technology (DOT) technique. We further investigated the effects of polymer molecular weights, location of biotin functionality within the polymer chain, and polymer chain conformations, that is, steric hindrance effects, on the binding numbers of biotinylated polymer chains per avidin within the polymer–protein bioconjugates, which were determined by the standard avidin/2‐(4‐hydroxyazobenzene)benzoic acid (HABA) assay. The binding numbers vary in the range of 1.9–3.3, depending on the molecular weights, locations of biotin functionality within synthetic polymer precursors, and polymer chain conformations.