Date of Award
Spring 5-19-2018
Degree Type
Thesis
Degree Name
MS Chemistry
Department
Chemistry and Biochemistry
Advisor
Joseph J. Badillo, Ph.D.
Committee Member
David Sabatino, Ph.D.
Committee Member
Cecilia Marzabadi, Ph.D.
Keywords
Bioconjugation, organocatalyst, Henry reaction, protein modification, site-selective.
Abstract
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.
Recommended Citation
Muneeswaran, Zilma Pereira, "Site-Selective Modification of Peptides and Proteins via Organocatalyzed Henry Reaction" (2018). Seton Hall University Dissertations and Theses (ETDs). 2533.
https://scholarship.shu.edu/dissertations/2533
Included in
Amino Acids, Peptides, and Proteins Commons, Enzymes and Coenzymes Commons, Medicinal and Pharmaceutical Chemistry Commons, Organic Chemicals Commons
