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Your search keyword '"Antevska, Aleksandra"' showing total 14 results
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14 results on '"Antevska, Aleksandra"'

5. Atomic View of Aqueous Cyclosporine A: Unpacking a Decades-Old Mystery

Author

Limbach, Miranda N., primary, Antevska, Aleksandra, additional, Oluwatoba, Damilola S., additional, Gray, Amber L. H., additional, Carroll, Xian B., additional, Hoffmann, Christina M., additional, Wang, Xiaoping, additional, Voehler, Markus W., additional, Steren, Carlos A., additional, and Do, Thanh D., additional

Published
2022
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7. Effects of Self-Assembly on the Photogeneration of Radical Cations in Halogenated Triphenylamines

Author

Hossain, Muhammad Saddam, primary, Sindt, Ammon J., additional, Goodlett, Dustin W., additional, Shields, Dylan J., additional, O’Connor, Colin J., additional, Antevska, Aleksandra, additional, Karakalos, Stavros G., additional, Smith, Mark D., additional, Garashchuk, Sophya, additional, Do, Thanh D., additional, Gudmundsdottir, Anna D., additional, and Shimizu, Linda S., additional

Published
2021
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13. Cytotoxicity of α-Helical, Staphylococcus aureusPSMα3 Investigated by Post-Ion-Mobility Dissociation Mass Spectrometry

Author

Gray, Amber L. H., Antevska, Aleksandra, Oluwatoba, Damilola S., Schonfeld, Grace E., Lazar Cantrell, Kristi L., and Do, Thanh D.

Abstract

Our knowledge of amyloid formation and cytotoxicity originating from self-assembly of α-helical peptides is incomplete. PSMα3 is the only system where high-resolution X-ray crystallography and toxicity data are available. Oligomers of multiple α-helical monomers are less stable than those of β-strands, partially due to the lack of a consistent hydrogen-bonding network. It is challenging to preserve such oligomers in the gas phase where mass-selected structural studies using ion-mobility spectrometry mass spectrometry (IMS-MS) could be performed. As the oligomers fall apart after exiting the drift cell of the mass spectrometer, novel features that have shorter (a loss of charged species) or longer (a loss of neutral species) arrival times than expected are present together with those from the intact species. By obtaining a complete data set of PSMα3 peptides in solution and with n-dodecyl-β-d-maltoside, a micelle-forming detergent, we are able to discern the dissociated from the intact oligomers and detergent-bound complexes and correlate the reported cytotoxicity to the peptide oligomeric structures and their interactions with membrane mimetics. The study sheds new insights into the interpretation of IMS-MS data from biomolecular self-assembly studies—an important and timely topic.

Published
2020
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