Enzymes are the foundation of any biological system, especially the human body. Their stability, great affinity and selectivity, catalytic efficiency, and reusability are just a few factors that distinguish enzymes from small molecules and make them ideal for pharmaceutical uses. While there has been much progress since the first use of enzymes as a treatment in the 1920’s, there are still many challenges that hinder the expansion in usage of this potent form of drugs. Our work stems from these challenges, such as instability at room temperature and degradation by the body’s proteolytic mechanisms, and seeks to use polymer conjugation to optimize enzyme properties for pharmaceutical uses. Polymers are ideal because they have specific controllable characteristics such as molecular weight, mechanical strength, and biocompatibility. <i>N</i>-Isopropylacrylamide (NIPAM) has thermoresponsive properties and has been shown to help increase stability of enzymes via conjugation. Furthermore, acrylic acid has pH-responsive properties and can increase the enzyme’s catalytic efficiency. NIPAM and acrylic acid-based homopolymers and copolymers have been synthesized using radical polymerization techniques. The enzyme we have chosen is lysozyme, which is easy to acquire, well characterized, and currently being developed as an antibiotic. It is functionalized with polymers through lysine residues using carbodiimide-mediated coupling. Polymers were coupled either through their end groups or pendant carboxylic acids within the main chain (Figure 1). The success of the conjugation was confirmed by gel electrophoresis and the thermal and kinetic properties of the bioconjugates were evaluated.

Synthesis and characterization of NIPAM and acrylic acid-based polymer-lysozyme conjugates

251st National Meeting (2016)

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