Biomolecular condensates formed by designer minimalistic peptides
The molecular mechanisms underlying the formation of biomolecular condensates have not been fully elucidated. Here the authors show that the LLPS propensity, dynamics, and encapsulation efficiency of designed peptide condensates can be tuned by subtle changes to the peptide composition.
Main Authors: | , , , , , , , , |
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Format: | Article |
Language: | English |
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Nature Portfolio
2023-01-01
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Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-023-36060-8 |
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author | Avigail Baruch Leshem Sian Sloan-Dennison Tlalit Massarano Shavit Ben-David Duncan Graham Karen Faulds Hugo E. Gottlieb Jordan H. Chill Ayala Lampel |
author_facet | Avigail Baruch Leshem Sian Sloan-Dennison Tlalit Massarano Shavit Ben-David Duncan Graham Karen Faulds Hugo E. Gottlieb Jordan H. Chill Ayala Lampel |
author_sort | Avigail Baruch Leshem |
collection | DOAJ |
description | The molecular mechanisms underlying the formation of biomolecular condensates have not been fully elucidated. Here the authors show that the LLPS propensity, dynamics, and encapsulation efficiency of designed peptide condensates can be tuned by subtle changes to the peptide composition. |
first_indexed | 2024-04-10T19:42:33Z |
format | Article |
id | doaj.art-f00422fac195453c853a9e060b8a14fb |
institution | Directory Open Access Journal |
issn | 2041-1723 |
language | English |
last_indexed | 2024-04-10T19:42:33Z |
publishDate | 2023-01-01 |
publisher | Nature Portfolio |
record_format | Article |
series | Nature Communications |
spelling | doaj.art-f00422fac195453c853a9e060b8a14fb2023-01-29T12:17:11ZengNature PortfolioNature Communications2041-17232023-01-0114111110.1038/s41467-023-36060-8Biomolecular condensates formed by designer minimalistic peptidesAvigail Baruch Leshem0Sian Sloan-Dennison1Tlalit Massarano2Shavit Ben-David3Duncan Graham4Karen Faulds5Hugo E. Gottlieb6Jordan H. Chill7Ayala Lampel8Shmunis School of Biomedicine and Cancer Research, George S. Wise Faculty of Life Sciences, Tel Aviv UniversityDepartment of Pure and Applied Chemistry, Technology and Innovation Centre, University of StrathclydeShmunis School of Biomedicine and Cancer Research, George S. Wise Faculty of Life Sciences, Tel Aviv UniversityShmunis School of Biomedicine and Cancer Research, George S. Wise Faculty of Life Sciences, Tel Aviv UniversityDepartment of Pure and Applied Chemistry, Technology and Innovation Centre, University of StrathclydeDepartment of Pure and Applied Chemistry, Technology and Innovation Centre, University of StrathclydeDepartment of Chemistry, Faculty of Exact Sciences, Bar Ilan UniversityDepartment of Chemistry, Faculty of Exact Sciences, Bar Ilan UniversityShmunis School of Biomedicine and Cancer Research, George S. Wise Faculty of Life Sciences, Tel Aviv UniversityThe molecular mechanisms underlying the formation of biomolecular condensates have not been fully elucidated. Here the authors show that the LLPS propensity, dynamics, and encapsulation efficiency of designed peptide condensates can be tuned by subtle changes to the peptide composition.https://doi.org/10.1038/s41467-023-36060-8 |
spellingShingle | Avigail Baruch Leshem Sian Sloan-Dennison Tlalit Massarano Shavit Ben-David Duncan Graham Karen Faulds Hugo E. Gottlieb Jordan H. Chill Ayala Lampel Biomolecular condensates formed by designer minimalistic peptides Nature Communications |
title | Biomolecular condensates formed by designer minimalistic peptides |
title_full | Biomolecular condensates formed by designer minimalistic peptides |
title_fullStr | Biomolecular condensates formed by designer minimalistic peptides |
title_full_unstemmed | Biomolecular condensates formed by designer minimalistic peptides |
title_short | Biomolecular condensates formed by designer minimalistic peptides |
title_sort | biomolecular condensates formed by designer minimalistic peptides |
url | https://doi.org/10.1038/s41467-023-36060-8 |
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