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Record W4413507247 · doi:10.1557/s43577-025-00938-3

Sequence enhances metal binding, assembly, and mechanics in DOPA-rich mussel proteins

2025· article· en· W4413507247 on OpenAlex

Why this work is in the frame

A frame that forgets how it found something cannot be audited. These are the routes that admitted this work.

affAt least one author lists a Canadian institution in the pinned OpenAlex snapshot.
fundA Canadian funder is recorded on the work.

Bibliographic record

VenueMRS Bulletin · 2025
Typearticle
Languageen
FieldMaterials Science
TopicPolymer Surface Interaction Studies
Canadian institutionsUniversité du Québec à MontréalMcGill University
FundersNatural Sciences and Engineering Research Council of CanadaMcGill UniversitySchweizerischer Nationalfonds zur Förderung der Wissenschaftlichen ForschungNational Science Foundation
KeywordsSequence (biology)MusselMolecular mechanicsComputational biologyNanotechnologyBiologyChemistryMaterials scienceBiochemistryEcologyComputational chemistryMolecular dynamics

Abstract

fetched live from OpenAlex

Abstract Mussel byssus is an established model for bioinspired design based on the discovery of 3,4-dihydroxyphenylalanine (DOPA)-mediated metal coordination cross-linking. Yet, synthetic mussel-inspired materials are inferior to native byssus. This stems from reductionist approaches in which the DOPA moiety is detached from its natural protein sequence and grafted onto polymers. Here, we investigated synthetic peptide derivatives of DOPA-rich protein mfp-1 to probe the role of amino acid sequence. Comparing the peptide to established mussel-inspired polethylene glycol (PEG)-DOPA polymers using spectroscopy and rheology, we found that peptide sequence strongly influences the pH at which DOPA-metal complexation forms, preference for specific metal ions (iron versus vanadium), and the mechanical properties of resulting materials. Moreover, we demonstrated that, mimicking natural assembly, mfp-1 peptides undergo sulfate-induced formation of fluid condensates that cross-linked preferentially with vanadium ions under acidic conditions relevant for native byssus formation. These findings provide new insights into byssus assembly and concepts for improved mussel-inspired materials. Graphical abstract Impact statement Organisms such as spiders and mussels fabricate biopolymeric materials with properties that outperform those made by humans. For example, the sticky fibers comprising the mussel byssus are as tough as Kevlar, have self-healing properties, and can adhere to wet surfaces with ease—something that our best glues fail to do. Moreover, the byssus is produced under biologically and environmentally friendly conditions using biorenewable building blocks. Researchers have attempted to mimic these properties in synthetic materials over the last two decades by copying the characteristic DOPA-catechol chemistry discovered in the byssus. Yet, currently, these many thousands of mussel-inspired materials do not match the native properties. Here, we explored the hypothesis that this could stem from reductionistic synthetic approaches that remove the DOPA moieties from the biochemical context of the protein sequence in which they evolved. We test this hypothesis by investigating the metal-binding capacity, self-assembly behavior, and mechanical performance of synthetic peptides that mimic the full consensus sequence of a prominent byssus protein—mfp-1. Our findings indicate that removing DOPA from its evolved biochemical environment yields inferior performance and processability, helping explain common challenges with current mussel-inspired materials. This finding will inspire mussel-inspired materials with improved properties.

Fetched live from OpenAlex and de-inverted. Abstracts are not stored in this database: the inverted indexes are 8.6 GB of the frame’s 9.3 GB of text, and the host has 13 GB free.

Full frame distilled prediction

Teacher imitation

Not calibrated prevalence, not ground truth. Human validation pending. Learned from the 10,348 direct Codex labels and 10,348 direct Gemma labels. Candidate is the union of thresholded teacher heads; consensus is their intersection. These outputs are machine_predicted_unvalidated and are not human labels or direct frontier model labels.

metaresearch head score (Codex)0.001
metaresearch head score (Gemma)0.000
Version: codex-gemma-dda1882f352aValidation status: machine_predicted_unvalidated
Candidate categoriesnone
Consensus categoriesnone
DomainCandidate signal: none · Consensus signal: none
Study designCandidate signal: Bench or experimental · Consensus signal: Bench or experimental
GenreCandidate signal: Empirical · Consensus signal: Empirical
Teacher disagreement score0.029
Threshold uncertainty score0.617

Codex and Gemma teacher scores by category

CategoryCodexGemma
Metaresearch0.0010.000
Meta-epidemiology (narrow)0.0000.000
Meta-epidemiology (broad)0.0000.000
Bibliometrics0.0000.000
Science and technology studies0.0000.000
Scholarly communication0.0000.000
Open science0.0000.000
Research integrity0.0000.000
Insufficient payload (model declined to judge)0.0000.000

Machine scores (provisional)

The two teacher heads of the student model, read on this work. A score orders the frame for review; it never asserts a category, and the validation status ships verbatim with every row.

Baseline scores from an immature model (maturity gate not passed, 7 training rounds). Scores rank; they never assert a category.

Opus teacher head0.019
GPT teacher head0.289
Teacher spread0.269 · how far apart the two teachers sit on this one work
Validation statusscore_only:v0-immature-baseline · verbatim from the scoring run: score_only means the number may rank works, and no category label ships from it