Evidence map›Paper›PMID 32427482›Full record

ArticleACS nano2020

Coassembly-Induced Transformation of Dipeptide Amyloid-Like Structures into Stimuli-Responsive Supramolecular Materials.

Wei Ji, Chengqian Yuan, Priyadarshi Chakraborty, Pandeeswar Makam, Santu Bera, Sigal Rencus-Lazar, Junbai Li, Xuehai Yan, Ehud Gazit

Open access · greenAbstract read
In one paragraph

Article in ACS nano, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
4.4field-weighted citation impact, top 4% 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

19 citing papers in PubMed, 95 citations in OpenAlex.

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  8. Evidence for SbioRxiv : the preprint server for biology · 2024
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  16. Modular Design of Supramolecular Ionic Peptides with Cell-Selective Membrane Activity.Chembiochem : a European journal of chemical biology · 2021
    Article
  17. 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

9 authors at 3 institutions in 2 countries.

Wei JiDepartment of Molecular Microbiology and Biotechnology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 6997801, Israel.ORCID 0000-0001-8982-5460
Chengqian YuanState Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences 100190 Beijing, China.
Priyadarshi ChakrabortyDepartment of Molecular Microbiology and Biotechnology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 6997801, Israel.ORCID 0000-0001-7174-7660
Pandeeswar MakamDepartment of Molecular Microbiology and Biotechnology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 6997801, Israel.
Santu BeraDepartment of Molecular Microbiology and Biotechnology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 6997801, Israel.ORCID 0000-0002-4830-552X
Sigal Rencus-LazarDepartment of Molecular Microbiology and Biotechnology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 6997801, Israel.
Junbai LiBeijing National Laboratory for Molecular Sciences, CAS Key Lab of Colloid Interface and Chemical Thermodynamics, Institute of Chemistry, Chinese Academy of Sciences, Beijing 100190, China.ORCID 0000-0001-9575-3125
Xuehai YanState Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences 100190 Beijing, China.ORCID 0000-0002-0890-0340
Ehud GazitDepartment of Molecular Microbiology and Biotechnology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 6997801, Israel.
Tel Aviv University · ILInstitute of Process Engineering · CNChinese Academy of Sciences · CN

Funding

European Research Council 694426
6 · The paper itself

Abstract

Conformational transition of proteins and peptides into highly stable, β-sheet-rich structures is observed in many amyloid-associated neurodegenerative disorders, yet the precise mechanism of amyloid formation at the molecular level remains poorly understood due to the complex molecular structures. Short peptides provide simplified models for studying the molecular basis of the assembly mechanism that governs β-sheet fibrillation processes underlying the formation and inhibition of amyloid-like structures. Herein, we report a supramolecular coassembly strategy for the inhibition and transformation of stable β-sheet-rich amyloid-derived dipeptide self-assemblies into adaptable secondary structural fibrillar assemblies by mixing with bipyridine derivatives. The interplay between the type and mixing ratio of bipyridine derivatives allowed the variable coassembly process with stimuli-responsive functional properties, studied by various experimental characterizations and computational methods. Furthermore, the resulting coassemblies showed functional redox- and photoresponsive properties, making them promising candidates for controllable drug release and fluorescent imprint. This work presents a coassembly strategy not only to explore the mechanism of amyloid-like structure formation and inhibition at the molecular level but also to manipulate amyloid-like structures into responsive supramolecular coassemblies for material science and biotechnology applications.

Indexed as

DipeptidesStimuli Responsive PolymersAmyloidAmyloidogenic ProteinsProtein Conformation, beta-StrandAmyloidAmyloidogenic ProteinsDipeptidesStimuli Responsive Polymersamyloid-like structuredipeptideself-assemblystimuli-responsivesupramolecular chemistry

Identifiers

PMID32427482
PMCPMC7616928
OpenAlexW3027179652

What OpenQuestion holds

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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.