PXD067305 is an
original dataset announced via ProteomeXchange.
Dataset Summary
| Title | Histidine-rich coiled-coils promote zinc-dependent self-assembly and curing of porous mussel glues |
| Description | Challenging to engineer in synthetic glues, wet adhesion is critical for many technical and biomedical applications. Mussels, however, have evolved underwater glues that adhere effectively onto slippery seashore surfaces. Past research on mussel adhesion highlights the importance of the post-translationally modified amino acid 3,4-dihydroxyphenylalanine (DOPA), found in abundance in mussel glue proteins. Yet, DOPA alone is insufficient to match native adhesion in synthetic mimics. Here, we provide evidence that a previously uncharacterized histidine-rich protein (mefp-12) plays a crucial role in the formation, curing, and likely performance of mussel glue. Biochemical analysis localizes mefp-12 within the vesicles in the mussel glue secretory glands, while AI-assisted modeling of its sequence predicts Zn-stabilized coiled coil conformation and several domains resembling zinc-finger motifs. In vitro investigation of a His-rich 𝛼-helical peptide from mefp-12 shows Zn- and pH-dependent liquid-liquid phase separation (LLPS), coalescence, and spreading over the substrate. Exposure to seawater pH induces subsequent self-assembly of the fluid condensates into solid nanoporous networks resembling the structure of the native mussel glue. Based on these findings we gain a deeper mechanistic understanding of mussel glue formation and function that challenges the dominant DOPA-centric paradigm, providing new inspiration for design of bio-inspired wet adhesives. |
| HostingRepository | PRIDE |
| AnnounceDate | 2026-01-19 |
| AnnouncementXML | Submission_2026-01-19_13:56:07.165.xml |
| DigitalObjectIdentifier | |
| ReviewLevel | Peer-reviewed dataset |
| DatasetOrigin | Original dataset |
| RepositorySupport | Unsupported dataset by repository |
| PrimarySubmitter | Mathieu Rivard |
| SpeciesList | scientific name: Mytilus edulis (Blue mussel); NCBI TaxID: NEWT:6550; |
| ModificationList | monohydroxylated residue; iodoacetic acid derivatized residue; deamidated residue |
| Instrument | Orbitrap Fusion |
Dataset History
| Revision | Datetime | Status | ChangeLog Entry |
| 0 | 2025-08-13 10:07:31 | ID requested | |
| ⏵ 1 | 2026-01-19 13:56:07 | announced | |
Publication List
Keyword List
| submitter keyword: coiled coil,mussel, adhesive, plaque, coacervate, histidine, zinc |
Contact List
| Matthew Harrington |
| contact affiliation | McGill University |
| contact email | matt.harrington@mcgill.ca |
| lab head | |
| Mathieu Rivard |
| contact affiliation | McGill University |
| contact email | mathieu.rivard2@mail.mcgill.ca |
| dataset submitter | |
Full Dataset Link List
Dataset FTP location
NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/01/PXD067305 |
| PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD067305
- Label: PRIDE project
- Name: Histidine-rich coiled-coils promote zinc-dependent self-assembly and curing of porous mussel glues