Multiphasic condensates formed with mono-component of tetrapeptides via phase separation
Abstract Biomolecular condensates, formed by liquid-liquid phase separation of biomacromolecules, play crucial roles in regulating physiological events in biological systems. While multiphasic condensates have been extensively studied, those derived from a single component of short peptides have not...
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2025-03-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-025-58060-6 |
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| _version_ | 1849389903623749632 |
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| author | Laicheng Zhou Longchen Zhu Cong Wang Tengyan Xu Jing Wang Bin Zhang Xin Zhang Huaimin Wang |
| author_facet | Laicheng Zhou Longchen Zhu Cong Wang Tengyan Xu Jing Wang Bin Zhang Xin Zhang Huaimin Wang |
| author_sort | Laicheng Zhou |
| collection | DOAJ |
| description | Abstract Biomolecular condensates, formed by liquid-liquid phase separation of biomacromolecules, play crucial roles in regulating physiological events in biological systems. While multiphasic condensates have been extensively studied, those derived from a single component of short peptides have not yet been reported. Here, we report the symmetrical core-shell structural biomolecular condensates formed with a programmable tetrapeptide library via phase separation. Our findings reveal that tryptophan is essential for core-shell structure formation due to its strongest homotypical π-π interaction, enabling us to modulate the structure of condensates from core-shell to homogeneous by altering the amino acid composition. Molecular dynamics simulation combined with cryogenic focused ion beam scanning electron microscopy and cryogenic electron microscopy show that the inner core of multiphasic tetrapeptide condensates is solid-like, consisting of ordered structures. The core is enveloped by a liquid-like shell, stabilizing the core structure. Furthermore, we demonstrate control over multiphasic condensate formation through intrinsic redox reactions or post-translational modifications, facilitating the rational design of synthetic multiphasic condensates for various applications on demand. |
| format | Article |
| id | doaj-art-432317a580d64edf918cc306cac9efda |
| institution | Kabale University |
| issn | 2041-1723 |
| language | English |
| publishDate | 2025-03-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj-art-432317a580d64edf918cc306cac9efda2025-08-20T03:41:49ZengNature PortfolioNature Communications2041-17232025-03-0116111410.1038/s41467-025-58060-6Multiphasic condensates formed with mono-component of tetrapeptides via phase separationLaicheng Zhou0Longchen Zhu1Cong Wang2Tengyan Xu3Jing Wang4Bin Zhang5Xin Zhang6Huaimin Wang7Department of Chemistry, Zhejiang UniversityDepartment of Chemistry, School of Science, Westlake UniversityDepartment of Chemistry, Massachusetts Institute of TechnologyDepartment of Chemistry, School of Science, Westlake UniversityDepartment of Chemistry, School of Science, Westlake UniversityDepartment of Chemistry, Massachusetts Institute of TechnologyDepartment of Chemistry, School of Science, Westlake UniversityDepartment of Chemistry, School of Science, Westlake UniversityAbstract Biomolecular condensates, formed by liquid-liquid phase separation of biomacromolecules, play crucial roles in regulating physiological events in biological systems. While multiphasic condensates have been extensively studied, those derived from a single component of short peptides have not yet been reported. Here, we report the symmetrical core-shell structural biomolecular condensates formed with a programmable tetrapeptide library via phase separation. Our findings reveal that tryptophan is essential for core-shell structure formation due to its strongest homotypical π-π interaction, enabling us to modulate the structure of condensates from core-shell to homogeneous by altering the amino acid composition. Molecular dynamics simulation combined with cryogenic focused ion beam scanning electron microscopy and cryogenic electron microscopy show that the inner core of multiphasic tetrapeptide condensates is solid-like, consisting of ordered structures. The core is enveloped by a liquid-like shell, stabilizing the core structure. Furthermore, we demonstrate control over multiphasic condensate formation through intrinsic redox reactions or post-translational modifications, facilitating the rational design of synthetic multiphasic condensates for various applications on demand.https://doi.org/10.1038/s41467-025-58060-6 |
| spellingShingle | Laicheng Zhou Longchen Zhu Cong Wang Tengyan Xu Jing Wang Bin Zhang Xin Zhang Huaimin Wang Multiphasic condensates formed with mono-component of tetrapeptides via phase separation Nature Communications |
| title | Multiphasic condensates formed with mono-component of tetrapeptides via phase separation |
| title_full | Multiphasic condensates formed with mono-component of tetrapeptides via phase separation |
| title_fullStr | Multiphasic condensates formed with mono-component of tetrapeptides via phase separation |
| title_full_unstemmed | Multiphasic condensates formed with mono-component of tetrapeptides via phase separation |
| title_short | Multiphasic condensates formed with mono-component of tetrapeptides via phase separation |
| title_sort | multiphasic condensates formed with mono component of tetrapeptides via phase separation |
| url | https://doi.org/10.1038/s41467-025-58060-6 |
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