Evidence map›Paper›PMID 33511004›Full record

ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2021

Evolution of Conformation, Nanomechanics, and Infrared Nanospectroscopy of Single Amyloid Fibrils Converting into Microcrystals.

Jozef Adamcik, Francesco Simone Ruggeri, Joshua T Berryman, Afang Zhang, Tuomas P J Knowles, Raffaele Mezzenga

Open access · goldAbstract read
In one paragraph

Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

15 citing papers in PubMed, 37 citations in OpenAlex.

  1. Single Amino Acid-Based Control of Fibril Supramolecular Chirality.The journal of physical chemistry letters · 2026
    Article
  2. Review
  3. Article
  4. Experimental methods for studying amyloid cross-interactions.Protein science : a publication of the Protein Society · 2025
    Review
  5. Article
  6. Article
  7. AFM Imaging Reveals MicroRNA-132 to be a Positive Regulator of Synaptic Functions.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  8. Article
  9. Article
  10. Review
  11. Mass Spectrometry Imaging of Biomaterials.Materials (Basel, Switzerland) · 2023
    Review
  12. Article
  13. Formation of amyloid loops in brain tissues is controlled by the flexibility of protofibril chains.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  14. Article
  15. Article
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

6 authors at 4 institutions in 4 countries.

Jozef AdamcikDepartment of Health Sciences and Technology ETH Zürich Zürich 8092 Switzerland.
Francesco Simone RuggeriDepartment of Chemistry University of Cambridge Lensfield Road Cambridge CB2 1EW UK.
Joshua T BerrymanUniversity of Luxembourg Department of Physics and Materials Science 162a Avenue de la Faïencerie Luxembourg L-1511 Luxembourg.
Afang ZhangShanghai University Department of Polymer Materials Nanchen Street 333 Shanghai 200444 China.
Tuomas P J KnowlesDepartment of Chemistry University of Cambridge Lensfield Road Cambridge CB2 1EW UK.
Raffaele MezzengaDepartment of Health Sciences and Technology ETH Zürich Zürich 8092 Switzerland.ORCID https://orcid.org/0000-0002-5739-2610
ETH Zurich · CHUniversity of Cambridge · GBShanghai University · CNUniversity of Luxembourg · LU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nanomechanical properties of amyloid fibrils and nanocrystals depend on their secondary and quaternary structure, and the geometry of intermolecular hydrogen bonds. Advanced imaging methods based on atomic force microscopy (AFM) have unravelled the morphological and mechanical heterogeneity of amyloids, however a full understanding has been hampered by the limited resolution of conventional spectroscopic methods. Here, it is shown that single molecule nanomechanical mapping and infrared nanospectroscopy (AFM-IR) in combination with atomistic modelling enable unravelling at the single aggregate scale of the morphological, nanomechanical, chemical, and structural transition from amyloid fibrils to amyloid microcrystals in the hexapeptides, ILQINS, IFQINS, and TFQINS. Different morphologies have different Young's moduli, within 2-6 GPa, with amyloid fibrils exhibiting lower Young's moduli compared to amyloid microcrystals. The origins of this stiffening are unravelled and related to the increased content of intermolecular

Indexed as

amyloid crystalsamyloid fibrilsamyloid polymorphismnanomechanical propertiessecondary structure

Identifiers

PMID33511004
PMCPMC7816722
OpenAlexW3111695388

What OpenQuestion holds

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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.