Laurier Chemistry-Biochemistry

Congratulations to our Dr. Stephen MacNeil on receiving Canada’s highest recognition for post-secondary educators, the 2025 3M National Teaching Fellowship! Read more in the university’s official news post below. 🥳🤩👨‍⚕️🎉🎈

Laurier’s Stephen MacNeil receives national 3M teaching award Stephen MacNeil, associate professor in Wilfrid Laurier University’s Chemistry and Biochemistry Department in the Faculty of Science, has been named a 2025 3M National Teaching Fellow. 

Laurier Partners with My Green Lab to Reduce Environmental Impact, Promote Sustainable Research

Read all about our newest green investments in our Chemistry & Biochemistry undergraduate teaching labs for a sustainable future!

Laurier partners with My Green Lab to reduce environmental impact, promote sustainable research | Wilfrid Laurier University Science and research labs at Wilfrid Laurier University have reduced water consumption by 98% and energy consumption of high-draw equipment by 30% by introducing new, more environmentally sustainable lab practices and processes. “Labs are fairly energy-intensive spaces,” says Gena Braun, researc...

Graduate student Starla Richardson will be competing in the AquaHacking Great Lakes Grand finale. Her team is developing carbon quantum dots from mealworm shells to detect lead in freshwater. Watch and vote for best pitch on May 10th at 1:30 PM EST on https://bit.ly/LiveGreatLakes

As part of Natural Sciences and Engineering Research Council of Canada \(NSERC\)'s Undergraduate Student Research Award program, Lorecha, Nikaela and Jordan gained valuable lab experience alongside Laurier faculty mentors.

Learn about the positive impacts they hope to make through their inspired research: https://ow.ly/M2oc50Qy4RL

Join us on Friday March 8 at 3:30 pm in N1044 (Science Building) for a seminar with Professor Zongchao Jia – Biomedical and Medical Sciences, Queen's University

Modification of Histidine- and Lysine-Rich Proteins by Inorganic Polyphosphate

Summary: Polyphosphate (polyP) is a pervasive biopolymer found in living organisms, characterized by linear chains of repeated phosphate units connected by high-energy phosphoanhydride bonds. Known for its diverse biological functions, polyP plays a key role in energy storage, phosphate buffering, and cellular regulation, influencing stress response, virulence, and longevity across various organisms. While its involvement in blood clotting and inflammation in humans is established, the molecular mechanisms remain elusive. Our laboratory recently unveiled a significant finding: proteins containing consecutive histidine and lysine residues exhibit a robust post-translational modification (PTM)-like interaction with polyP. Notably, this polyP modification, dependent on histidine/lysine residues, is non-covalent yet remarkably resilient under harsh denaturing conditions—a characteristic shared with covalent PTMs. Through extensive screening, we have identified many polyP-modified proteins in humans, yeast, and bacteria. Importantly, our research demonstrates that polyP modifications play a pivotal role in regulating diverse protein functions. For instance, modification of histidine-repeat proteins disrupts phase separation and the phosphorylation activity of the human protein kinase DYRK1A, while inhibiting the activity of the transcription factor MafB. Furthermore, polyP modification of lysine-repeat proteins, such as SrmB and EngA, is implicated in the virulence of Pseudomonas aeruginosa.

Join us on Friday, March 1 at 3:30 p.m. in N1044 (Science Building) for a seminar with Professor Graeme Howe - Department of Chemistry, Queen's University

Genome mining for "extremozymes" - Extremophiles as sources of novel biocatalysts

Directed evolution has enabled the development of extremely useful biocatalysts that have, in some cases, supplanted traditional organic chemistry in the industrial production of value-added commodity chemicals. Generally, mutations introduced into a protein scaffold to increase catalytic efficiency are accompanied by a compensatory destabilization of the enzyme. To circumvent this issue and allow a more thorough exploration of sequence space around naturally occurring enzymes, we have turned to sequence similarity networks (SSNs) to mine the genomes of thermophilic microorganisms to identify novel thermostable variants of enzymes with potential industrial utility. These networks allow for the exploration of whole protein families and the interrelatedness of every member sequence through an ‘all-by-all’ BLAST. Through the iterative construction of SSNs with varying sequence identity cutoffs, we have produced networks of putative isofunctional clusters that allow a single sequence with known catalytic function to reveal the role of thousands of unannotated PETase-like genes.
Our initial efforts in this arena have focused on the search for new thermostable plastic-degrading enzymes as a part of the OpenPlastic consortium’s efforts to develop a circular plastics economy. Following the initial discovery of a cutinase-like enzyme from Ideonella sakaiensis that degrades polyethylene terephthalate (PET), there has been an explosion in research revolving around the biocatalytic degradation of PET and other plastics. While several engineered PETases have emerged that are sufficiently stable and catalytically efficient for industrial PET degradation, we opted to direct our initial efforts to exploit the wealth of PETase sequence-function relationships to mine the genomes of extremophiles for new PETases as starting points for further engineering efforts. Using the I. sakaiensis enzyme as a seed sequence, SSNs were constructed that led to the identification of 10 putative PETases from bacteria with optimal growth temperatures ranging from 50 °C to 80 °C. This presentation will detail our efforts to characterize these enzymes and their potential utility in the degradation of PET plastics. Similar bioinformatics-driven approaches to identify and characterize thermostable enzymes that degrade polyamides and polyurethanes will also be presented.

We are looking for an Assistant Professor - Biochemistry

To learn more and apply:

Assistant Professor - Chemistry and Biochemistry (Biochemistry) Assistant Professor - Chemistry and Biochemistry (Biochemistry)

We are looking for an Assistant Professor - Theoretical/Computational Chemistry

To learn more and apply:

Assistant Professor - Chemistry/Biochemistry (Theoretical/Computational Chemistry) Assistant Professor - Chemistry/Biochemistry (Theoretical/Computational Chemistry)

Taking place tomorrow!

Friday, January 12 at 3:30pm
Career Options in Chemistry & Biochemistry
Speaker: Lisa Roy, Further Education & Employment Consultant
Career Centre
Join the presentation in-person (N1044) or through Zoom (link was sent to all Chem and Biochem majors, but you can also contact Dr. Dawe if you did not receive an email).

Join us on Friday, January 19 at 3:30 p.m. in N1044 (Science Building) for a seminar with Professor Stefania Impellizzeri, Chemistry and Biology, Toronto Metropolitan University

Of MOFs and MEF: Hybrid Strategies for Fluorescence Enhancement

ABSTRACT:
The synergistic integration of materials with organic fluorophores enables the development of innovative photoresponsive systems that would not otherwise be accessible through their separate organic and inorganic components alone. For instance, the encapsulation of dyes in metal-organic frameworks (MOFs) can lead to the creation of emissive nanocomposites in which the guest probe is bestowed with outstanding photophysical properties such as high photostability, quantum yield, and lifetime, meanwhile providing a convenient solution to issues related to low biocompatibility, scarce solubility in water or aggregation-induced quenching, without complicating the synthesis.
On the other hand, the interaction of organic emitters with metallic nanostructures (such as silver nanoparticles) can modify emission in ways not seen in classical fluorescence, resulting in an increased rate of excitation as well as a higher radiative decay rate of nearby fluorophores, in accordance with the principles of metal-enhanced fluorescence (MEF). In this context, single-molecule fluorescence microscopy can provide unique insights into the MEF mechanism which are hidden by ensemble-averaged measurements, demonstrating that the fusion between classic spectroscopic techniques and single-molecule methods can bring remarkable advantages for quantitatively characterizing particle-molecule interactions. This knowledge and methodology can be used to tailor MEF to meet the needs of different applications, such as those requiring maximum enhancement of fluorescence intensity or instead prioritizing excited-state photochemistry.

Friday, January 12 at 3:30pm
Career Options in Chemistry & Biochemistry
Speaker: Lisa Roy, Further Education & Employment Consultant
Career Centre
Join the presentation in-person (N1044) or through Zoom (link was sent to all Chem and Biochem majors, but you can also contact Dr. Dawe if you did not receive an email).

New course for W24 - SC201: Drugs, Dyes, and Displays with instructor Dr. Ken Maly! Learn about the food we eat, clothes we wear, medications, and the screen you are looking at right now! No prior chemistry knowledge (not even high school chemistry) is required. CRN 3845