Assembly of transmembrane pores from mirror-image peptides

Alpha-helix nanopores have a range of potential applications and the inclusion of non-natural amino acids allows for modification. Here, the authors report on the creation of alpha-helix pores using D-amino acids and show the pores formed, have different properties to the L-counterparts and were res...

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Main Authors: Smrithi Krishnan R, Kalyanashis Jana, Amina H. Shaji, Karthika S. Nair, Anjali Devi Das, Devika Vikraman, Harsha Bajaj, Ulrich Kleinekathöfer, Kozhinjampara R. Mahendran
Format: Article
Language:English
Published: Nature Portfolio 2022-09-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-022-33155-6
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author Smrithi Krishnan R
Kalyanashis Jana
Amina H. Shaji
Karthika S. Nair
Anjali Devi Das
Devika Vikraman
Harsha Bajaj
Ulrich Kleinekathöfer
Kozhinjampara R. Mahendran
author_facet Smrithi Krishnan R
Kalyanashis Jana
Amina H. Shaji
Karthika S. Nair
Anjali Devi Das
Devika Vikraman
Harsha Bajaj
Ulrich Kleinekathöfer
Kozhinjampara R. Mahendran
author_sort Smrithi Krishnan R
collection DOAJ
description Alpha-helix nanopores have a range of potential applications and the inclusion of non-natural amino acids allows for modification. Here, the authors report on the creation of alpha-helix pores using D-amino acids and show the pores formed, have different properties to the L-counterparts and were resistant to proteases.
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spelling doaj.art-00435f5b33224b8c8b398bd0b815eb652022-12-22T04:30:41ZengNature PortfolioNature Communications2041-17232022-09-0113111310.1038/s41467-022-33155-6Assembly of transmembrane pores from mirror-image peptidesSmrithi Krishnan R0Kalyanashis Jana1Amina H. Shaji2Karthika S. Nair3Anjali Devi Das4Devika Vikraman5Harsha Bajaj6Ulrich Kleinekathöfer7Kozhinjampara R. Mahendran8Membrane Biology Laboratory, Transdisciplinary Research Program, Rajiv Gandhi Centre for BiotechnologyDepartment of Physics and Earth Sciences, Jacobs University BremenMembrane Biology Laboratory, Transdisciplinary Research Program, Rajiv Gandhi Centre for BiotechnologyMicrobial Processes and Technology Division, CSIR- National Institute for Interdisciplinary Science and Technology (NIIST)Membrane Biology Laboratory, Transdisciplinary Research Program, Rajiv Gandhi Centre for BiotechnologyMembrane Biology Laboratory, Transdisciplinary Research Program, Rajiv Gandhi Centre for BiotechnologyMicrobial Processes and Technology Division, CSIR- National Institute for Interdisciplinary Science and Technology (NIIST)Department of Physics and Earth Sciences, Jacobs University BremenMembrane Biology Laboratory, Transdisciplinary Research Program, Rajiv Gandhi Centre for BiotechnologyAlpha-helix nanopores have a range of potential applications and the inclusion of non-natural amino acids allows for modification. Here, the authors report on the creation of alpha-helix pores using D-amino acids and show the pores formed, have different properties to the L-counterparts and were resistant to proteases.https://doi.org/10.1038/s41467-022-33155-6
spellingShingle Smrithi Krishnan R
Kalyanashis Jana
Amina H. Shaji
Karthika S. Nair
Anjali Devi Das
Devika Vikraman
Harsha Bajaj
Ulrich Kleinekathöfer
Kozhinjampara R. Mahendran
Assembly of transmembrane pores from mirror-image peptides
Nature Communications
title Assembly of transmembrane pores from mirror-image peptides
title_full Assembly of transmembrane pores from mirror-image peptides
title_fullStr Assembly of transmembrane pores from mirror-image peptides
title_full_unstemmed Assembly of transmembrane pores from mirror-image peptides
title_short Assembly of transmembrane pores from mirror-image peptides
title_sort assembly of transmembrane pores from mirror image peptides
url https://doi.org/10.1038/s41467-022-33155-6
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