Search

Your search keyword '"Gunnoo, Smita B."' showing total 13 results
Start Over Author "Gunnoo, Smita B."
13 results on '"Gunnoo, Smita B."'

2. Engineering Chirally Blind Protein Pseudocapsids into Antibacterial Persisters

Author

Kepiro, Ibolya E., primary, Marzuoli, Irene, additional, Hammond, Katharine, additional, Ba, Xiaoliang, additional, Lewis, Helen, additional, Shaw, Michael, additional, Gunnoo, Smita B., additional, De Santis, Emiliana, additional, Łapińska, Urszula, additional, Pagliara, Stefano, additional, Holmes, Mark A., additional, Lorenz, Christian D., additional, Hoogenboom, Bart W., additional, Fraternali, Franca, additional, and Ryadnov, Maxim G., additional

Published
2019
Full Text
View/download PDF

5. Engineering Chirally Blind Protein Pseudocapsids into Antibacterial Persisters

Author

Kepiro, Ibolya E., Marzuoli, Irene, Hammond, Katharine, Ba, Xiaoliang, Lewis, Helen, Shaw, Michael, Gunnoo, Smita B., De Santis, Emiliana, Łapińska, Urszula, Pagliara, Stefano, Holmes, Mark A., Lorenz, Christian D., Hoogenboom, Bart W., Fraternali, Franca, and Ryadnov, Maxim G.

Abstract

Antimicrobial resistance stimulates the search for antimicrobial forms that may be less subject to acquired resistance. Here we report a conceptual design of protein pseudocapsids exhibiting a broad spectrum of antimicrobial activities. Unlike conventional antibiotics, these agents are effective against phenotypic bacterial variants, while clearing “superbugs” in vivowithout toxicity. The design adopts an icosahedral architecture that is polymorphic in size, but not in shape, and that is available in both land depimeric forms. Using a combination of nanoscale and single-cell imaging we demonstrate that such pseudocapsids inflict rapid and irreparable damage to bacterial cells. In phospholipid membranes they rapidly convert into nanopores, which remain confined to the binding positions of individual pseudocapsids. This mechanism ensures precisely delivered influxes of high antimicrobial doses, rendering the design a versatile platform for engineering structurally diverse and functionally persistent antimicrobial agents.

Published
2020
Full Text
View/download PDF

11. Methods for converting cysteine to dehydroalanine on peptides and proteins

Author

Chalker, Justin M., primary, Gunnoo, Smita B., additional, Boutureira, Omar, additional, Gerstberger, Stefanie C., additional, Fernández-González, Marta, additional, Bernardes, Gonçalo J. L., additional, Griffin, Laura, additional, Hailu, Hanna, additional, Schofield, Christopher J., additional, and Davis, Benjamin G., additional

Published
2011
Full Text
View/download PDF

12. Engineering Chirally Blind Protein Pseudocapsids into Antibacterial Persisters

Author

Maxim G. Ryadnov, Smita B. Gunnoo, Franca Fraternali, Xiaoliang Ba, Mark A. Holmes, Emiliana De Santis, Helen Lewis, Ibolya E. Kepiro, Michael Shaw, Katharine Hammond, Urszula Łapińska, Stefano Pagliara, Irene Marzuoli, Bart W. Hoogenboom, Christian D. Lorenz, Kepiro, Ibolya E [0000-0002-8934-3389], Marzuoli, Irene [0000-0001-7536-6144], Hammond, Katharine [0000-0002-3755-6489], Ba, Xiaoliang [0000-0002-3882-3585], Lewis, Helen [0000-0002-9993-0640], Shaw, Michael [0000-0001-6099-3217], Gunnoo, Smita B [0000-0002-7435-8377], De Santis, Emiliana [0000-0002-0943-6586], Łapińska, Urszula [0000-0003-3593-9248], Pagliara, Stefano [0000-0001-9796-1956], Holmes, Mark A [0000-0002-5454-1625], Lorenz, Christian D [0000-0003-1028-4804], Hoogenboom, Bart W [0000-0002-8882-4324], Fraternali, Franca [0000-0002-3143-6574], Ryadnov, Maxim G [0000-0003-4847-1154], and Apollo - University of Cambridge Repository

Subjects
Models, Molecular, Protein Folding, Multidrug tolerance, medicine.drug_class, Cell Survival, Surface Properties, Antibiotics, Protein design, nanopores, General Physics and Astronomy, 02 engineering and technology, Microbial Sensitivity Tests, 010402 general chemistry, Protein Engineering, 01 natural sciences, Broad spectrum, Acquired resistance, Antibiotic resistance, medicine, Escherichia coli, General Materials Science, antimicrobial resistance, Particle Size, protein design, artificial pseudocapsids, Chemistry, General Engineering, 021001 nanoscience & nanotechnology, Antimicrobial, 0104 chemical sciences, Anti-Bacterial Agents, superbugs, persister cells, Biophysics, 0210 nano-technology, Antimicrobial Cationic Peptides
Abstract

Antimicrobial resistance stimulates the search for antimicrobial forms that may be less subject to acquired resistance. Here we report a conceptual design of protein pseudocapsids exhibiting a broad spectrum of antimicrobial activities. Unlike conventional antibiotics, these agents are effective against phenotypic bacterial variants, while clearing "superbugs" in vivo without toxicity. The design adopts an icosahedral architecture that is polymorphic in size, but not in shape, and that is available in both l and d epimeric forms. Using a combination of nanoscale and single-cell imaging we demonstrate that such pseudocapsids inflict rapid and irreparable damage to bacterial cells. In phospholipid membranes they rapidly convert into nanopores, which remain confined to the binding positions of individual pseudocapsids. This mechanism ensures precisely delivered influxes of high antimicrobial doses, rendering the design a versatile platform for engineering structurally diverse and functionally persistent antimicrobial agents.

Published
2020

13. Visible-Light-Mediated Selective Arylation of Cysteine in Batch and Flow.

Author

Bottecchia C, Rubens M, Gunnoo SB, Hessel V, Madder A, and Noël T

Abstract

A mild visible-light-mediated strategy for cysteine arylation is presented. The method relies on the use of eosin Y as a metal-free photocatalyst and aryldiazonium salts as arylating agents. The reaction can be significantly accelerated in a microflow reactor, whilst allowing the in situ formation of the required diazonium salts. The batch and flow protocol described herein can be applied to obtain a broad series of arylated cysteine derivatives and arylated cysteine-containing dipeptides. Moreover, the method was applied to the chemoselective arylation of a model peptide in biocompatible reaction conditions (room temperature, phosphate-buffered saline (PBS) buffer) within a short reaction time., (© 2017 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA.)

Published
2017
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results