Controlling Supramolecular Assembly through Peptide Chirality
Peptide-based self-assembled hydrogels are promising materials for diverse applications due to their biocompatibility, tunable mechanical properties, and ability to form nanostructured networks via noncovalent interactions. One of the most extensively studied hydrogelators, fluorenylmethyloxycarbony...
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2025
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| _version_ | 1849927634628116480 |
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| author | Manosree Chatterjee (5641505) |
| author2 | Itzhak Grinberg (10586537) Santu Bera (1769386) Dana Cohen-Gerassi (9248439) Oren Ben-Zvi (3406775) Iftach Yacoby (45454) Moran Aviv (5820032) Lihi Adler-Abramovich (1328061) |
| author2_role | author author author author author author author |
| author_facet | Manosree Chatterjee (5641505) Itzhak Grinberg (10586537) Santu Bera (1769386) Dana Cohen-Gerassi (9248439) Oren Ben-Zvi (3406775) Iftach Yacoby (45454) Moran Aviv (5820032) Lihi Adler-Abramovich (1328061) |
| author_role | author |
| dc.creator.none.fl_str_mv | Manosree Chatterjee (5641505) Itzhak Grinberg (10586537) Santu Bera (1769386) Dana Cohen-Gerassi (9248439) Oren Ben-Zvi (3406775) Iftach Yacoby (45454) Moran Aviv (5820032) Lihi Adler-Abramovich (1328061) |
| dc.date.none.fl_str_mv | 2025-11-25T12:25:23Z |
| dc.identifier.none.fl_str_mv | 10.1021/acsami.5c14913.s002 |
| dc.relation.none.fl_str_mv | https://figshare.com/articles/media/Controlling_Supramolecular_Assembly_through_Peptide_Chirality/30705593 |
| dc.rights.none.fl_str_mv | CC BY-NC 4.0 info:eu-repo/semantics/openAccess |
| dc.subject.none.fl_str_mv | Biophysics Biochemistry Biotechnology Immunology Space Science Biological Sciences not elsewhere classified Chemical Sciences not elsewhere classified transparent fibrillary gels heteroenantiomeric systems exhibited extensively studied hydrogelators 3d hydrogel capable fast gelation results drug delivery applications diverse applications due tunable mechanical properties four enantiomeric forms sensitive enzyme hydrogenase 2 </ sub peptide chirality peptide developing peptide hydrogels slower gelation may controlling supramolecular assembly various applications faster gelation supramolecular nanostructures structural properties enantiomeric design peptide self sensitive processes sensitive biomolecules chirality plays chirality influences turbid nanospheres small molecules promising materials phase transition nanofiber networks morphological transitions hydrogels formed homogeneous distribution heterogeneous structures findings highlight encapsulating enzymes encapsulated within density cavities critical role attractive candidate assembly kinetics assembled hydrogels analytical techniques |
| dc.title.none.fl_str_mv | Controlling Supramolecular Assembly through Peptide Chirality |
| dc.type.none.fl_str_mv | Dataset Media info:eu-repo/semantics/publishedVersion dataset |
| description | Peptide-based self-assembled hydrogels are promising materials for diverse applications due to their biocompatibility, tunable mechanical properties, and ability to form nanostructured networks via noncovalent interactions. One of the most extensively studied hydrogelators, fluorenylmethyloxycarbonyl-diphenylalanine (Fmoc-FF), rapidly self-assembles into a 3D hydrogel capable of encapsulating enzymes and proteins, making it an attractive candidate for drug delivery applications and the protection of oxygen-sensitive biomolecules. However, its fast gelation results in heterogeneous structures and low-density cavities, limiting its uniformity and complicating the handling. Chirality plays a critical role in peptide self-assembly, yet its impact on hydrogel functionality remains underexplored. Here, we investigate how chirality influences the self-assembly kinetics, morphology, and structural properties of all four enantiomeric forms of Fmoc-FF. Using a range of analytical techniques, we tracked the morphological transitions from monomers to supramolecular nanostructures. Hydrogels formed from homoenantiomers displayed greater rigidity and faster gelation, while heteroenantiomeric systems exhibited a slower, three-phase transition from turbid nanospheres to transparent fibrillary gels. This slower gelation may be advantageous for controlled encapsulation, allowing for homogeneous distribution of the cargo. Finally, all enantiomeric hydrogels effectively prevented oxygen diffusion through their nanofiber networks, allowing H<sub>2</sub> production by the oxygen-sensitive enzyme hydrogenase, which was encapsulated within the hydrogels. These findings highlight the potential of enantiomeric design in developing peptide hydrogels for various applications, particularly the encapsulation of small molecules and large proteins as well as oxygen-sensitive processes. |
| eu_rights_str_mv | openAccess |
| id | Manara_3331665292ceecb3ad8e453f543963f2 |
| identifier_str_mv | 10.1021/acsami.5c14913.s002 |
| network_acronym_str | Manara |
| network_name_str | ManaraRepo |
| oai_identifier_str | oai:figshare.com:article/30705593 |
| publishDate | 2025 |
| repository.mail.fl_str_mv | |
| repository.name.fl_str_mv | |
| repository_id_str | |
| rights_invalid_str_mv | CC BY-NC 4.0 |
| spelling | Controlling Supramolecular Assembly through Peptide ChiralityManosree Chatterjee (5641505)Itzhak Grinberg (10586537)Santu Bera (1769386)Dana Cohen-Gerassi (9248439)Oren Ben-Zvi (3406775)Iftach Yacoby (45454)Moran Aviv (5820032)Lihi Adler-Abramovich (1328061)BiophysicsBiochemistryBiotechnologyImmunologySpace ScienceBiological Sciences not elsewhere classifiedChemical Sciences not elsewhere classifiedtransparent fibrillary gelsheteroenantiomeric systems exhibitedextensively studied hydrogelators3d hydrogel capablefast gelation resultsdrug delivery applicationsdiverse applications duetunable mechanical propertiesfour enantiomeric formssensitive enzyme hydrogenase2 </ subpeptide chirality peptidedeveloping peptide hydrogelsslower gelation maycontrolling supramolecular assemblyvarious applicationsfaster gelationsupramolecular nanostructuresstructural propertiesenantiomeric designpeptide selfsensitive processessensitive biomoleculeschirality playschirality influencesturbid nanospheressmall moleculespromising materialsphase transitionnanofiber networksmorphological transitionshydrogels formedhomogeneous distributionheterogeneous structuresfindings highlightencapsulating enzymesencapsulated withindensity cavitiescritical roleattractive candidateassembly kineticsassembled hydrogelsanalytical techniquesPeptide-based self-assembled hydrogels are promising materials for diverse applications due to their biocompatibility, tunable mechanical properties, and ability to form nanostructured networks via noncovalent interactions. One of the most extensively studied hydrogelators, fluorenylmethyloxycarbonyl-diphenylalanine (Fmoc-FF), rapidly self-assembles into a 3D hydrogel capable of encapsulating enzymes and proteins, making it an attractive candidate for drug delivery applications and the protection of oxygen-sensitive biomolecules. However, its fast gelation results in heterogeneous structures and low-density cavities, limiting its uniformity and complicating the handling. Chirality plays a critical role in peptide self-assembly, yet its impact on hydrogel functionality remains underexplored. Here, we investigate how chirality influences the self-assembly kinetics, morphology, and structural properties of all four enantiomeric forms of Fmoc-FF. Using a range of analytical techniques, we tracked the morphological transitions from monomers to supramolecular nanostructures. Hydrogels formed from homoenantiomers displayed greater rigidity and faster gelation, while heteroenantiomeric systems exhibited a slower, three-phase transition from turbid nanospheres to transparent fibrillary gels. This slower gelation may be advantageous for controlled encapsulation, allowing for homogeneous distribution of the cargo. Finally, all enantiomeric hydrogels effectively prevented oxygen diffusion through their nanofiber networks, allowing H<sub>2</sub> production by the oxygen-sensitive enzyme hydrogenase, which was encapsulated within the hydrogels. These findings highlight the potential of enantiomeric design in developing peptide hydrogels for various applications, particularly the encapsulation of small molecules and large proteins as well as oxygen-sensitive processes.2025-11-25T12:25:23ZDatasetMediainfo:eu-repo/semantics/publishedVersiondataset10.1021/acsami.5c14913.s002https://figshare.com/articles/media/Controlling_Supramolecular_Assembly_through_Peptide_Chirality/30705593CC BY-NC 4.0info:eu-repo/semantics/openAccessoai:figshare.com:article/307055932025-11-25T12:25:23Z |
| spellingShingle | Controlling Supramolecular Assembly through Peptide Chirality Manosree Chatterjee (5641505) Biophysics Biochemistry Biotechnology Immunology Space Science Biological Sciences not elsewhere classified Chemical Sciences not elsewhere classified transparent fibrillary gels heteroenantiomeric systems exhibited extensively studied hydrogelators 3d hydrogel capable fast gelation results drug delivery applications diverse applications due tunable mechanical properties four enantiomeric forms sensitive enzyme hydrogenase 2 </ sub peptide chirality peptide developing peptide hydrogels slower gelation may controlling supramolecular assembly various applications faster gelation supramolecular nanostructures structural properties enantiomeric design peptide self sensitive processes sensitive biomolecules chirality plays chirality influences turbid nanospheres small molecules promising materials phase transition nanofiber networks morphological transitions hydrogels formed homogeneous distribution heterogeneous structures findings highlight encapsulating enzymes encapsulated within density cavities critical role attractive candidate assembly kinetics assembled hydrogels analytical techniques |
| status_str | publishedVersion |
| title | Controlling Supramolecular Assembly through Peptide Chirality |
| title_full | Controlling Supramolecular Assembly through Peptide Chirality |
| title_fullStr | Controlling Supramolecular Assembly through Peptide Chirality |
| title_full_unstemmed | Controlling Supramolecular Assembly through Peptide Chirality |
| title_short | Controlling Supramolecular Assembly through Peptide Chirality |
| title_sort | Controlling Supramolecular Assembly through Peptide Chirality |
| topic | Biophysics Biochemistry Biotechnology Immunology Space Science Biological Sciences not elsewhere classified Chemical Sciences not elsewhere classified transparent fibrillary gels heteroenantiomeric systems exhibited extensively studied hydrogelators 3d hydrogel capable fast gelation results drug delivery applications diverse applications due tunable mechanical properties four enantiomeric forms sensitive enzyme hydrogenase 2 </ sub peptide chirality peptide developing peptide hydrogels slower gelation may controlling supramolecular assembly various applications faster gelation supramolecular nanostructures structural properties enantiomeric design peptide self sensitive processes sensitive biomolecules chirality plays chirality influences turbid nanospheres small molecules promising materials phase transition nanofiber networks morphological transitions hydrogels formed homogeneous distribution heterogeneous structures findings highlight encapsulating enzymes encapsulated within density cavities critical role attractive candidate assembly kinetics assembled hydrogels analytical techniques |