Click Chemistry: A Powerful Tool to Create Polymer‐Based Macromolecular Chimeras

Abstract

The combination of polymeric with biological materials, to create biohybrid macromolecules that merge the properties of both the natural and synthetic components, is a flourishing area in both life sciences and biotechnology. The click chemistry philosophy has recently provided a powerful tool in this direction, leading to a plethora of novel, tailor‐made biomacromolecules with unprecedented structural characteristics and properties. The different synthetic strategies, using the alkyne–azide click cycloadditions to bioorthogonally achieve the coupling of synthetic polymers with nucleic acids, peptides, sugars, proteins or even viruses and cells is described. The review covers the latest developments in this very dynamic and rapidly expanding field.magnified image

Hybrid Block Copolymers Constituted by Peptides and Synthetic Polymers: An Overview of Synthetic Approaches, Supramolecular Behavior and Potential Applications

“…Strategies for the preparation of peptide/protein-polymer conjugates can for example be split into those formulated for producing peptides/proteins bearing chemoselective groups and those formulated to introduce chemoselective handles into synthetic polymers. For more detailed information on the synthesis of polymer bioconjugates via the ligation of peptides, proteins, oligonucleotides/nucleic acids or carbohydrates on synthetic polymers the reader is directed to reviews of Gauthier and Klok [7], Lutz and Börner [4], and Le Drournaguet and Velonia [8]. For the different synthetic approaches towards peptide-polymer and protein-polymer block copolymers, reviews of Klok [9], and Marsden and Kros [10], or the book chapter of Deming [11] are specially recommended.…”

Synthesis of Heterobifunctional Protein Fusions Using Copper‐Free Click Chemistry and the Aldehyde Tag

“…[46][47][48] Furthermore, the approach can be extended to protein-synthetic polymer conjugations and surface immobilization [49,50] along with designing protein conjugates that extend serum halflife, [51] or for vaccine development. [52] Experimental Section General protein conjugation: A buffered solution (optimal pH 4.5) of aldehyde-tagged protein (10-50 mm) was treated with aminooxy reagent (0.2-1 mm, 10-20 equiv) and agitated at 35 8C for 16 h. Proteins were purified from low molecular weight reagents by buffer exchange or analyzed directly by SDS-PAGE.…”

Design of Polyvalent Polymer Therapeutics

“…Fortunately, there has been an increasing interest among polymer scientists in developing and taking advantage of ''click'' chemistry reactions [82] for modifying polymers [41,83,84]. Some of these methods are the topic of other chapters within this book.…”