MétaCan
Menu
Back to cohort

Identification of Ni2+-binding peptides in sunflower meal protein hydrolysate for deeper understanding of peptide-metal interactions

2025· article· en· W4408279059 on OpenAlexaff
Jairo Andrés Camaño Echavarría, Christelle Mathé, Jean‐Michel Girardet, Cédric Paris, Chibuike C. Udenigwe, Katalin Selmeczi, Laetitia Canabady‐Rochelle

Bibliographic record

VenueJournal of Inorganic Biochemistry · 2025
Typearticle
Languageen
FieldBiochemistry, Genetics and Molecular Biology
TopicProtein Hydrolysis and Bioactive Peptides
Canadian institutionsUniversity of Ottawa
FundersInstitut National de Recherche pour l'Agriculture, l'Alimentation et l'EnvironnementAgence Nationale de la RechercheMinistère de l'Enseignement Supérieur et de la RechercheUniversité de Lorraine
KeywordsChemistryHydrolysatePeptideSunflowerIdentification (biology)BiochemistryBotany

Abstract

fetched live from OpenAlex

Sunflower ( Helianthus annus L.) is one of the most important oil crops in the world. Once oil extracted, sunflower meal by-product could offer a potential alternative for various food applications due to its high protein content. Derived from food protein hydrolysates, metal-binding peptides have attracted attention as bioactive compounds to prevent metal-induced oxidation and diseases. This study aimed to investigate the Ni 2+ -binding ability of sunflower meal protein hydrolysates and ten peptides theoretically present in sunflower proteins using IMAC, switchSENSE®, UV–vis and CD techniques. Single and sequential enzymatic treatments were applied to produce hydrolysates using Protamex® (Prot) and Protamex followed by Flavourzyme® (Prot+Flav), respectively. MS/MS analysis of enriched Ni 2+ -binding peptides fractions revealed different composition of His-containing peptides among hydrolysates; however, similar to the His-containing pure peptides, the Ni 2+ -binding ability of all the hydrolysates was almost identical in IMAC. On the contrary, switchSENSE® studies indicated that the Ni 2+ -binding ability of sunflower peptides does not depend only on the presence of His residues, but also on their position along the polypeptide chain and the presence of proline, suggesting that Prot hydrolysates exhibited the highest Ni 2+ -binding ability. UV–vis and CD data confirmed that sunflower peptides bound onto Ni 2+ through nitrogen atoms from imidazole sidechain of His residues, deprotonated amide bonds and N-terminal amino group, indicating square-planar and also octahedral geometries in the formed complexes. Finally, His-containing peptides without proline could offer a suitable strategy to design metal-binding peptides from sunflower meal by-product, with the most promising motifs being LL H VT and WL H. Derived from food protein hydrolysates, metal-binding peptides have attracted attention as bioactive compounds to prevent metal-induced oxidation and diseases. This study aimed to investigate the Ni 2+ -binding ability of sunflower meal protein hydrolysates and ten peptides theoretically present in sunflower proteins using IMAC, switchSENSE®, UV–vis and CD techniques. • IMAC and switchSENSE® unveiled the chelating profile of peptides and hydrolysates. • Sunflower meal-derived peptides complexed Ni 2+ with 3 N and 4 N coordination modes. • Single hydrolysate possessed the strongest ability to complex Ni 2+ with ATCUN motif. • WLH and LLHVT ATCUN peptides identified as the most interesting Ni 2+ chelator. • 26 metal-chelating peptides with His identified from sunflower meal hydrolysates.

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.

How this classification was reachedexpand

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 score0.006
Threshold uncertainty score0.624

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 head0.013
GPT teacher head0.271
Teacher spread0.258 · 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

Classification

machine, unvalidated

Machine predicted; a candidate call from one teacher head, not a consensus.

The models applied no category: nothing in the taxonomy fit this work.
Study designBench or experimental
Domainnot available
GenreEmpirical

How this classification was reached, model by model and score by score, is at the end of the page under "How this classification was reached".

Quick stats

Citations4
Published2025
Admission routes1
Has abstractyes

Explore more

Same venueJournal of Inorganic BiochemistrySame topicProtein Hydrolysis and Bioactive PeptidesFrench-language works237,207