Evidence map›Paper›PMID 34938993›Full record

ArticleMaterials today. Bio2022

Functional amyloid-chitin hybrid ink coupled with flexible fabrication approaches for diverse macro and micro-structures.

Shicao Wei, Yingfeng Li, Ke Li, Anqi Kang, Siyu Zhang, Teng Feng, Hui Zhang, Chao Zhong

Open access · goldAbstract read
In one paragraph

Article in Materials today. Bio, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.4field-weighted citation impact, top 42% 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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed, 8 citations in OpenAlex.

  1. Review
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 1 country.

Shicao WeiMaterials and Physical Biology Division, School of Physical Science and Technology, ShanghaiTech University, Shanghai, 201210, China.
Yingfeng LiMaterials and Physical Biology Division, School of Physical Science and Technology, ShanghaiTech University, Shanghai, 201210, China.
Ke LiMaterials and Physical Biology Division, School of Physical Science and Technology, ShanghaiTech University, Shanghai, 201210, China.
Anqi KangMaterials and Physical Biology Division, School of Physical Science and Technology, ShanghaiTech University, Shanghai, 201210, China.
Siyu ZhangMaterials and Physical Biology Division, School of Physical Science and Technology, ShanghaiTech University, Shanghai, 201210, China.
Teng FengSchool of Life Science and Technology, ShanghaiTech University, Shanghai, 201210, China.
Hui ZhangSchool of Life Science and Technology, ShanghaiTech University, Shanghai, 201210, China.
Chao ZhongMaterials and Physical Biology Division, School of Physical Science and Technology, ShanghaiTech University, Shanghai, 201210, China.
ShanghaiTech University · CNChinese Academy of Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The precise fabrication of artificially designed molecular complexes into ordered structures resembling their natural counterparts would find broad applications but remains a major challenge in the field. Here we genetically design chitin-binding domain (CBD)-containing amyloid proteins, and rationally fabricate well-ordered CBD-containing functional amyloid-chitin complex structures by coupling a top-down manufacturing process with a bottom-up self-assembly. Our fabrication approach starts with the dissolution of both CBD-containing functional amyloid and chitin in hexafluoroisopropanol (HFIP) to make a hybrid ink. This hybrid ink platform, coupled with multiple fabrication methods including airbrushing, electrospinning and soft-lithography, produces a series of unique freestanding structures. The structural features of the products, such as the ability to direct the light path and mimicking of the extracellular matrix enable applications in functional light gratings and cell culture, respectively. Further genetic engineering of the protein component allowed tunable functionalization of these materials, including nanoparticle immobilization and protein conjugation, resulting in broad applications in electronic devices and enzyme immobilization. Our technological platform can drive new advances in biocatalysis, tissue engineering, biomedicine, photonics and electronics.

Indexed as

Bio-fabricationCompositesFunctional amyloidPolysaccharideProtein Self-assembly

Identifiers

PMID34938993
PMCPMC8661696
OpenAlexW4200525152

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.