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.

Bibliographic Details
Main Authors: Avigail Baruch Leshem, Sian Sloan-Dennison, Tlalit Massarano, Shavit Ben-David, Duncan Graham, Karen Faulds, Hugo E. Gottlieb, Jordan H. Chill, Ayala Lampel
Format: Article
Language:English
Published: Nature Portfolio 2023-01-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-023-36060-8
_version_ 1828051690117398528
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
work_keys_str_mv AT avigailbaruchleshem biomolecularcondensatesformedbydesignerminimalisticpeptides
AT siansloandennison biomolecularcondensatesformedbydesignerminimalisticpeptides
AT tlalitmassarano biomolecularcondensatesformedbydesignerminimalisticpeptides
AT shavitbendavid biomolecularcondensatesformedbydesignerminimalisticpeptides
AT duncangraham biomolecularcondensatesformedbydesignerminimalisticpeptides
AT karenfaulds biomolecularcondensatesformedbydesignerminimalisticpeptides
AT hugoegottlieb biomolecularcondensatesformedbydesignerminimalisticpeptides
AT jordanhchill biomolecularcondensatesformedbydesignerminimalisticpeptides
AT ayalalampel biomolecularcondensatesformedbydesignerminimalisticpeptides