Protein-polymer hybrids are inspiring materials that provide advancements in many areas, such as biomolecular delivery, therapeutics, antibacterial materials, catalysis, energy, and fundamental protein sciences. While exciting features and great potentials have been shown in these antimicrobial materials, there are several barriers that prevent further development of the hybrid materials. For example, in order to precisely control the products of the protein-polymer conjugation reactions so that the properties of the materials can be controlled, it is important to understand the effects of polymer length, conjugation sites, abundance and conformation, as well as the structure of the protein upon conjugation. In this work, we intend to bridge the previously missed gap by attaching a single polymer chain to different sites of T4L, one at a time, and investigate the effect of attachment site on secondary structure and activity.  The protein site being studied will be mutated to a cysteine, and one end of the polymer will be modified to a maleimide group.  The reaction of the polymer and an active thiol will create a stable covalent bond. Herein we probe the effect of polymer length and location of PEGylated-T4 lysozyme (T4L) and revealed the reasons of activity loss for such antimicrobial hybrids. Our results demonstrate the importance of attachment sites on hybrid stability and activity and suggested an effective approach to design antimicrobial hybrids.

Effects of polymer conjugation site on the functionality of an antimicrobial protein-polymer hybrid

2019 Spring National Meeting

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