@article{galiakhmetov_davern_esteves_awosanya_guthrie_proulx_nevzorov_2022, title={Aligned peptoid-based macrodiscs for structural studies of membrane proteins by oriented-sample NMR}, volume={121}, ISSN={["1542-0086"]}, DOI={10.1016/j.bpj.2022.07.024}, abstractNote={Development of a robust, uniform, and magnetically orientable lipid mimetic will undoubtedly advance solid-state NMR of macroscopically aligned membrane proteins. Here, we report on a novel lipid membrane mimetic based on peptoid belts. The peptoids, composed of 15 residues, were synthesized by alternating N-(2-phenethyl)glycine with N-(2-carboxyethyl)glycine residues at a 2:1 molar ratio. The chemically synthesized peptoids possess a much lower degree of polydispersity versus styrene-maleic acid polymers, thus yielding uniform discs. Moreover, the peptoid oligomers are more flexible and do not require a specific folding, unlike lipoproteins, in order to wrap around the hydrophobic membrane core. The NMR spectra measured for the membrane-bound form of Pf1 coat protein incorporated in this new lipid mimetics demonstrate a higher order parameter and uniform linewidths compared with the conventional bicelles and peptide-based macrodiscs. Importantly, unlike bicelles, the peptoid-based macrodiscs are detergent free.}, number={17}, journal={BIOPHYSICAL JOURNAL}, author={Galiakhmetov, Azamat R. and Davern, Carolynn M. and Esteves, Richard J. A. and Awosanya, Emmanuel O. and Guthrie, Quibria A. E. and Proulx, Caroline and Nevzorov, Alexander A.}, year={2022}, month={Sep}, pages={3263–3270} }
 @article{young_guthrie_proulx_2020, title={N-Arylation of Amino Acid Esters to Expand Side Chain Diversity in Ketoxime Peptide Ligations}, volume={85}, ISSN={["1520-6904"]}, DOI={10.1021/acs.joc.9b02810}, abstractNote={Palladium-catalyzed N-arylations of amino acid tert-butyl esters using 4-bromo-N,N-dimethylaniline as a coupling partner are reported. The resulting N-aryl amino acid esters are suitable building blocks for the synthesis of electron-rich N-aryl peptides, which undergo oxidative couplings to aminooxy groups to afford ketoxime peptides under mild conditions. N-aryl amino acid tert-butyl esters possessing unnatural side chains were also accessed via glycine Schiff base alkylation, further increasing the scope of Cα-substitution in ketoxime peptides.}, number={3}, journal={JOURNAL OF ORGANIC CHEMISTRY}, author={Young, Hailey A. and Guthrie, Quibria A. E. and Proulx, Caroline}, year={2020}, month={Feb}, pages={1748–1755} }
 @article{guthrie_young_proulx_2019, title={Ketoxime peptide ligations: oxidative couplings of alkoxyamines to N-aryl peptides}, volume={10}, ISSN={["2041-6539"]}, DOI={10.1039/c9sc04028e}, abstractNote={Ketoxime peptides are readily accessible from oxidative couplings between N-aryl peptides and alkoxyamines under catalyst-free conditions.}, number={41}, journal={CHEMICAL SCIENCE}, author={Guthrie, Quibria A. E. and Young, Hailey A. and Proulx, Caroline}, year={2019}, month={Nov}, pages={9506–9512} }
 @article{guthrie_proulx_2018, title={Oxime Ligation via in situ Oxidation of N-Phenylglycinyl Peptides}, volume={20}, ISSN={["1523-7052"]}, DOI={10.1021/acs.orglett.8b00713}, abstractNote={Mild conditions for oxime ligations via in situ generation of α-imino amide intermediates are reported. The evaluation of a variety of N-terminal N-phenylglycine residues revealed that a metal-free, chemoselective oxidation was possible using oxygen as the only oxidant in buffer at pH 7.0. Moreover, selective unmasking of an inert residue by addition of potassium ferricyanide is demonstrated. These simple and mild conditions, which can be fine-tuned by the electronic properties of the N-phenylglycine residue, offer unique advantages over conventional approaches for oxime ligations.}, number={9}, journal={ORGANIC LETTERS}, author={Guthrie, Quibria A. E. and Proulx, Caroline}, year={2018}, month={May}, pages={2564–2567} }