Date of Award
Chemistry and Biochemistry
Joseph J. Badillo, Ph.D.
David Sabatino, Ph.D.
Cecilia Marzabadi, Ph.D.
Bioconjugation, organocatalyst, Henry reaction, protein modification, site-selective.
In this research, peptides and protein containing serine on the N-terminus underwent site-selective modification following organocatalyzed bioconjugation that offered an additional functional group. It was shown that transforming the N-terminus serine to an aldehyde allowed site-specific bioconjugation to occur by utilizing the well-known Henry reaction. This method also grants a safer pathway for bioconjugation utilizing “green-chemistry” and biocompatible conditions. Amino acids and amino acid derived organocatalysts were utilized in the Henry reaction resulting in yields of up to 86 % conversion. Promising preliminary results were achieved in this research using peptides and myoglobin as the bioconjugation targets. Further investigation to be performed includes the analysis of the final product, as well as, applying this methodology to a number of other proteins.
Muneeswaran, Zilma Pereira, "Site-Selective Modification of Peptides and Proteins via Organocatalyzed Henry Reaction" (2018). Seton Hall University Dissertations and Theses (ETDs). 2533.