Novel protein immobilization approaches for the development of vaccine candidates and enzymatic reactors

Abstract

Protein immobilization on solid supports offers a wide range of opportunities in the biotech industry. Its many possible applications in diverse fields cover from enzyme immobilization promoting an enhancement in the physicochemical properties, to vaccine candidate generation, reducing the associated production costs and improving the immunogenic performance of the vaccine candidate. The immobilization process implicates profound science in both substrate surface and proteins. Proteins are composed of amino acids polymerized jointly through the formation of peptide bonds. One or more polypeptide chains fold into a 3- dimensional (3-D) bioactive protein, with many exposed functional groups such as carboxyl, amine, hydroxyl, and sulfhydryl. Regarding the immobilization strategy, the conformation of the immobilized protein needs to be seriously considered. In the enzyme field, the active site is usually a groove or pocket where the target or substrate molecules bind and experience a chemical reaction. In order to function properly, this active site needs to be in specific and appropriate conformation and accessible to the target. The present study explores two fundamentally different methods for protein immobilization: the IC-Tagging methodology using a modified viral protein, and 3D printing thought the use of Stereolithography (SLA). We investigate the feasibility of these strategies and its efficiency in generating properly folded immobilized proteins for different applications in the field of biocatalysts and cancer immunotherapy.