Chemistry Seminar Series: Joelle PelletierExport this event to calendar

Wednesday, September 4, 2019 — 9:00 AM EDT

Transglutaminase-mediated protein labelling: successes and challenges

Joelle N. Pelletier
Professor of Chemistry
Adjunct Professor of Biochemistry
Université de Montréal

Wednesday, September 4, 2019
9:00 a.m.
C2-361 (Reading Room)

Abstract

Engineering enzyme-catalyzed reactions can be achieved by modifying substrates and conditions to provide routes to non-native reactivity, and valuable products. The microbial transglutaminase enzyme (MTG) has been heavily used in the food industry for decades, as a texturant.  MTG efficiently catalyzes the normally costly and atom-expensive formation of amide bonds, typically between proteins, using the gamma-carboxamide group of glutamine and the ε-amino group of lysine. However, it can be diverted to include synthetic amine-bearing substrates, thus expanding the amide-bond forming utility of MTG in protein labelling. We demonstrate that various non-native, small-molecule amines react efficiently with MTG. We will present the MTG-catalyzed formation of synthetically attractive, non-native amides such as proteins modified with alkyne, azide, cyclooctene, cyclooctyne and tetrazine-type reagents. Our work further examines the scope and limitations of introducing new substrates for MTG-catalyzed bioorthogonal protein labelling reactions, including antibody fragments.

 

Location 
C2 - Chemistry 2
Room 361
200 University Avenue West

Waterloo, ON N2L 3G1
Canada

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