Evidence map›Paper›PMID 38368506›Full record

ArticleBiophysical journal2024

Improving cryo-EM grids for amyloid fibrils using interface-active solutions and spectator proteins.

Dylan Valli, Saik Ann Ooi, Giorgio Scattolini, Himanshu Chaudhary, Alesia A Tietze, Michał Maj

Open access · hybridAbstract read
In one paragraph

Article in Biophysical journal, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

6 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. A structural model of toxic amyloid oligomers involved in type 2 diabetes.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Article
  5. The Structure of Human IAPP Fibrils Reflects Membrane and pH Conditions.Journal of the American Chemical Society · 2025
    Article
  6. 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 2 institutions in 1 country.

Dylan ValliDepartment of Chemistry - Ångström Laboratory, Uppsala University, Uppsala, Sweden.
Saik Ann OoiDepartment of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.
Giorgio ScattoliniDepartment of Chemistry - Ångström Laboratory, Uppsala University, Uppsala, Sweden.
Himanshu ChaudharyDepartment of Chemistry - Ångström Laboratory, Uppsala University, Uppsala, Sweden.
Alesia A TietzeDepartment of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.
Michał MajDepartment of Chemistry - Ångström Laboratory, Uppsala University, Uppsala, Sweden. Electronic address: michal.maj@kemi.uu.se.
Uppsala University · SEUniversity of Gothenburg · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Preparation of cryoelectron microscopy (cryo-EM) grids for imaging of amyloid fibrils is notoriously challenging. The human islet amyloid polypeptide (hIAPP) serves as a notable example, as the majority of reported structures have relied on the use of nonphysiological pH buffers, N-terminal tags, and seeding. This highlights the need for more efficient, reproducible methodologies that can elucidate amyloid fibril structures formed under diverse conditions. In this work, we demonstrate that the distribution of fibrils on cryo-EM grids is predominantly determined by the solution composition, which is critical for the stability of thin vitreous ice films. We discover that, among physiological pH buffers, HEPES uniquely enhances the distribution of fibrils on cryo-EM grids and improves the stability of ice layers. This improvement is attributed to direct interactions between HEPES molecules and hIAPP, effectively minimizing the tendency of hIAPP to form dense clusters in solutions and preventing ice nucleation. Furthermore, we provide additional support for the idea that denatured protein monolayers forming at the interface are also capable of eliciting a surfactant-like effect, leading to improved particle coverage. This phenomenon is illustrated by the addition of nonamyloidogenic rat IAPP (rIAPP) to a solution of preaggregated hIAPP just before the freezing process. The resultant grids, supplemented with this "spectator protein", exhibit notably enhanced coverage and improved ice quality. Unlike conventional surfactants, rIAPP is additionally capable of disentangling the dense clusters formed by hIAPP. By applying the proposed strategies, we have resolved the structure of the dominant hIAPP polymorph, formed in vitro at pH 7.4, to a final resolution of 4 Å. The advances in grid preparation presented in this work hold significant promise for enabling structural determination of amyloid proteins which are particularly resistant to conventional grid preparation techniques.

Indexed as

AmyloidIceAnimalsCryoelectron MicroscopyHEPESHumansIslet Amyloid PolypeptideRatsAmyloidHEPESIceIslet Amyloid Polypeptide

Identifiers

PMID38368506
PMCPMC10995402
OpenAlexW4392256716

What OpenQuestion holds

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LicenceCC BY
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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.