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...
Main Authors: | , , , , , , , , |
---|---|
Format: | Article |
Language: | English |
Published: |
Nature Portfolio
2022-09-01
|
Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-022-33155-6 |
_version_ | 1797995007807848448 |
---|---|
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. |
first_indexed | 2024-04-11T09:54:40Z |
format | Article |
id | doaj.art-00435f5b33224b8c8b398bd0b815eb65 |
institution | Directory Open Access Journal |
issn | 2041-1723 |
language | English |
last_indexed | 2024-04-11T09:54:40Z |
publishDate | 2022-09-01 |
publisher | Nature Portfolio |
record_format | Article |
series | Nature Communications |
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 |
work_keys_str_mv | AT smrithikrishnanr assemblyoftransmembraneporesfrommirrorimagepeptides AT kalyanashisjana assemblyoftransmembraneporesfrommirrorimagepeptides AT aminahshaji assemblyoftransmembraneporesfrommirrorimagepeptides AT karthikasnair assemblyoftransmembraneporesfrommirrorimagepeptides AT anjalidevidas assemblyoftransmembraneporesfrommirrorimagepeptides AT devikavikraman assemblyoftransmembraneporesfrommirrorimagepeptides AT harshabajaj assemblyoftransmembraneporesfrommirrorimagepeptides AT ulrichkleinekathofer assemblyoftransmembraneporesfrommirrorimagepeptides AT kozhinjampararmahendran assemblyoftransmembraneporesfrommirrorimagepeptides |