Cationic Surface Charge Engineering of Recombinant Transthyretin Remarkably Increases the Inhibitory Potency Against Amyloid β-Protein Fibrillogenesis.

Xiaoding Lin, Ting Xu, Wenqi Hou, Xiaoyan Dong, Yan Sun

Abstract read

In one paragraph

Article in Molecules (Basel, Switzerland), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it

0cells of the map it votes in

0citing papers in PubMed

–field-weighted citation impact

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

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3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

5 authors.

Xiaoding LinKey Laboratory of Systems Bioengineering and Frontiers Science Center for Synthetic Biology (Ministry of Education), Department of Biochemical Engineering, School of Chemical Engineering and Technology, Tianjin University, Tianjin 300350, China.ORCID 0000-0002-8712-174X

Ting XuKey Laboratory of Systems Bioengineering and Frontiers Science Center for Synthetic Biology (Ministry of Education), Department of Biochemical Engineering, School of Chemical Engineering and Technology, Tianjin University, Tianjin 300350, China.ORCID 0009-0001-5271-9696

Wenqi HouKey Laboratory of Systems Bioengineering and Frontiers Science Center for Synthetic Biology (Ministry of Education), Department of Biochemical Engineering, School of Chemical Engineering and Technology, Tianjin University, Tianjin 300350, China.

Xiaoyan DongKey Laboratory of Systems Bioengineering and Frontiers Science Center for Synthetic Biology (Ministry of Education), Department of Biochemical Engineering, School of Chemical Engineering and Technology, Tianjin University, Tianjin 300350, China.

Yan SunKey Laboratory of Systems Bioengineering and Frontiers Science Center for Synthetic Biology (Ministry of Education), Department of Biochemical Engineering, School of Chemical Engineering and Technology, Tianjin University, Tianjin 300350, China.ORCID 0000-0001-5256-9571

Funding

National Natural Science Foundation of China 22178259

6 · The paper itself

Abstract

The deposition of amyloid β-protein (Aβ) in the brain is the main pathogenesis of Alzheimer's disease (AD). The development of potent inhibitors against Aβ aggregation is one of the effective strategies to combat AD. Endogenous transthyretin (TTR) can inhibit Aβ fibrillization via hydrophobic interactions, but its weak inhibitory potency hinders its application in AD therapy. Here, different recombinant TTRs were designed by cationic surface charge engineering. Compared with TTR, all positively charged recombinant TTRs showed enhanced capability in inhibiting Aβ aggregation, especially the recombinant protein obtained by mutating the acidic amino acid in TTR to arginine (TTR-nR) exhibited excellent inhibitory effect. Among them, TTR-7R remarkably increased the inhibitory potency against Aβ, which could effectively inhibit Aβ

Indexed as

Amyloid beta-PeptidesPrealbuminRecombinant ProteinsAlzheimer DiseaseAnimalsCationsCell SurvivalHumansHydrophobic and Hydrophilic InteractionsProtein EngineeringStatic ElectricityAmyloid beta-PeptidesCationsPrealbuminRecombinant ProteinsAlzheimer’s diseaseamyloidosisamyloid β-proteininhibitorsrecombinant proteintransthyretin

Identifiers

PMID39519665

DOI10.3390/molecules29215023

PMCPMC11547489

What OpenQuestion holds

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LicenceCC BY

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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.