It is widely accepted that vaccines are valuable preparations for prevention against life-threatening diseases such as polio, measles and smallpox and their utilization led to control and/or eradication of aforementioned infectious diseases. Common drawbacks in classical vaccine formulations led to the development of less allergenic and more specific peptide vaccines that usually consist of 20-30 amino acids and an external adjuvant to enhance immunogenicity of peptide epitopes, which are normally weak antigens and could therefore not always initiate an immune response. However, these adjuvants involving chemical substances and biomolecules, might cause allergic reactions, similar to those of infectious agents and/or whole antigens in classical vaccines. Hence, adjuvant free but potent peptide vaccines are required. Here, I will discuss two recent publications on how to decrease the allergenic effects of adjuvants via covalent bonding utilizing chemoselective selenoester ligation chemistry (Mc Donald et al. ACS Chem. Biol., 2018, ASAP) as well as how serendipity influences vaccine design exemplified by self-adjuvating peptoid vaccines (Szekely et al. J. Med. Chem, 2018, 61, 9568-9582).
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Contributed by Can Araman
Can Araman completed his PhD degree under the supervision of Prof. Christian Becker at the University of Vienna. During this period, he worked on the semisynthesis of prion protein variants carrying glycan mimics and investigated their biophysical/biochemical properties in vitro. Currently, he is working as a postdoctoral researcher at the Leiden Institute of Chemistry (Netherlands), Bioorganic Synthesis Division under the guidance of Dr. Sander van Kasteren. His research interests are directed towards to the study kinetics of antigen processing & presentation using bioorthogonal chemistry as well as semisynthesis of posttranslationally modified antigens.