Evidence map›Paper›PMID 34931493›Full record

ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2022

Oat Plant Amyloids for Sustainable Functional Materials.

Jiangtao Zhou, Ting Li, Mohammad Peydayesh, Mattia Usuelli, Viviane Lutz-Bueno, Jie Teng, Li Wang, Raffaele Mezzenga

Registry-linked trialOpen access · goldAbstract read
In one paragraph

Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT05826899 (A Stable Isotope Study in Young Iron-depleted Thai Women to Evaluate the Bioavailability of an Oat Protein-based Iron Delivery System), which is not on this map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
10.1field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

NCT05826899 nacompletednot on this mapstarted 2023, after this paper: background citation

A Stable Isotope Study in Young Iron-depleted Thai Women to Evaluate the Bioavailability of an Oat Protein-based Iron Delivery System

TypeinterventionalSponsorThe Rainforest CompanyRan2023 to 2024Enrolled52ConditionsBioavailabilityArms54Fe SO4, 57Fe Oat-1, 58Fe Oat-2, 54 FeSO4 + Acai puree with honey, 57Fe Oat-1 + Acai puree with honey
3 · Its place in the literature

Who cites it

31 citing papers in PubMed, 111 citations in OpenAlex.

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  15. Biowaste-Derived Triboelectric Nanogenerators for Emerging Bioelectronics.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 2 countries.

Jiangtao ZhouDepartment of Health Sciences and Technology, ETH Zurich, Zurich, 8092, Switzerland.
Ting LiSchool of Food Science and Technology, National Engineering Laboratory for Cereal Fermentation Technology, Jiangnan University, Lihu Road 1800, Wuxi, 214122, China.
Mohammad PeydayeshDepartment of Health Sciences and Technology, ETH Zurich, Zurich, 8092, Switzerland.
Mattia UsuelliDepartment of Health Sciences and Technology, ETH Zurich, Zurich, 8092, Switzerland.
Viviane Lutz-BuenoDepartment of Health Sciences and Technology, ETH Zurich, Zurich, 8092, Switzerland.
Jie TengDepartment of Health Sciences and Technology, ETH Zurich, Zurich, 8092, Switzerland.
Li WangSchool of Food Science and Technology, National Engineering Laboratory for Cereal Fermentation Technology, Jiangnan University, Lihu Road 1800, Wuxi, 214122, China.
Raffaele MezzengaDepartment of Health Sciences and Technology, ETH Zurich, Zurich, 8092, Switzerland.ORCID 0000-0002-5739-2610
ETH Zurich · CHJiangnan University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amyloid functional materials from amyloid fibril building blocks, produced in vitro from amyloidogenic natural proteins or synthetic peptides, show diverse functionalities ranging from environmental science and biomedicine, to nanotechnology and biomaterials. However, sustainable and affordable sources of amyloidogenic proteins remain the bottleneck for large-scale applications, and to date, interest remains essentially limited to fundamental studies. Plant-derived proteins would be an ideal source due to their natural abundance and low environmental impact. Hereby oat globulin, the primary protein of oat plant (Avena sativa), is utilized to yield high-quality amyloid fibrils and functional materials based thereof. These fibrils show a rich multistranded ribbon-like polymorphism and a fibrillization process with both irreversible and reversible pathways. The authors furthermore fabricate oat-amyloid aerogels, films, and membranes for possible use in water purification, sensors, and patterned electrodes. The sustainability footprint of oat-amyloids against other protein sources is demonstrated, anticipating an environmentally-efficient platform for advanced materials and technologies.

Indexed as

AmyloidAmyloidogenic ProteinsAmyloidosisAvenaNanotechnologyPlant ProteinsAmyloidAmyloidogenic ProteinsPlant Proteinsamyloid fibrilsfunctional amyloid materialsplant proteinreversible amyloidsustainability

Identifiers

PMID34931493
PMCPMC8811842
OpenAlexW4200347550

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.