Evidence map›Paper›PMID 30275931›Full record

ArticleNano research2018

Nanoscale inhibition of polymorphic and ambidextrous IAPP amyloid aggregation with small molecules.

Aleksandr Kakinen, Jozef Adamcik, Bo Wang, Xinwei Ge, Raffaele Mezzenga, Thomas P Davis, Feng Ding, Pu Chun Ke

Open access · bronzeAbstract read
In one paragraph

Article in Nano research, 2018. 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
3.0field-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

19 citing papers in PubMed, 44 citations in OpenAlex.

  1. Review
  2. Formation of a β-Endorphin Corona Mitigates Alzheimer's Amyloidogenesis.Small (Weinheim an der Bergstrasse, Germany) · 2025
    Article
  3. Article
  4. Article
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  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Mitigation of Amyloidosis with Nanomaterials.Advanced materials (Deerfield Beach, Fla.) · 2020
    Review
  13. AuNational science review · 2020
    Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Mitigating Human IAPP Amyloidogenesis In Vivo with Chiral Silica Nanoribbons.Small (Weinheim an der Bergstrasse, Germany) · 2018
    Article
  19. 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

8 authors at 4 institutions in 4 countries.

Aleksandr KakinenARC Centre of Excellence in Convergent Bio-Nano Science and Technology, Monash Institute of Pharmaceutical Sciences, Monash University, 381 Royal Parade, Parkville, VIC 3052, Australia.
Jozef AdamcikFood & Soft Materials, Department of Health Science & Technology, ETH Zurich, Schmelzbergstrasse 9, LFO, E23, 8092 Zurich, Switzerland.
Bo WangDepartment of Physics and Astronomy, Clemson University, Clemson, SC 29634, USA.
Xinwei GeDepartment of Physics and Astronomy, Clemson University, Clemson, SC 29634, USA.
Raffaele MezzengaFood & Soft Materials, Department of Health Science & Technology, ETH Zurich, Schmelzbergstrasse 9, LFO, E23, 8092 Zurich, Switzerland.
Thomas P DavisARC Centre of Excellence in Convergent Bio-Nano Science and Technology, Monash Institute of Pharmaceutical Sciences, Monash University, 381 Royal Parade, Parkville, VIC 3052, Australia.
Feng DingDepartment of Physics and Astronomy, Clemson University, Clemson, SC 29634, USA.
Pu Chun KeARC Centre of Excellence in Convergent Bio-Nano Science and Technology, Monash Institute of Pharmaceutical Sciences, Monash University, 381 Royal Parade, Parkville, VIC 3052, Australia.
Clemson University · USETH Zurich · CHMonash University · AUUniversity of Warwick · GB

Funding

Inhibition of Human Islet Amyloid Polypeptide AggregationR35GM119691 · NIGMS · CLEMSON UNIVERSITY · PI DING, FENG · 2016 to 2020
$1.9M
NIGMS NIH HHS R35 GM119691
6 · The paper itself

Abstract

Understanding how small molecules interface amyloid fibrils on the nanoscale is of importance for developing therapeutic treatment against amyloid-based diseases. Here we show, for the first time, that human islet amyloid polypeptide (IAPP) in the fibrillar form is polymorphic and ambidextrous possessing multiple periodicities. Upon interfacing with small molecule epigallocatechin gallate (EGCG), IAPP aggregation was rendered off pathway assuming the form of soft and disordered clusters, while mature IAPP fibrils displayed kinks and branching but conserved the twisted fibril morphology. These nanoscale phenomena resulted from competitive interactions between EGCG and the IAPP amyloidogenic region, as well as end capping of the fibrils by the small molecule. This information is crucial to delineating IAPP toxicity implicated in type 2 diabetes and developing new inhibitors against amyloidogenesis.

Indexed as

DMD simulationsIAPP fibrillizationinhibitionpersistence lengthsmall molecule

Identifiers

PMID30275931
PMCPMC6162064
OpenAlexW2772750159

What OpenQuestion holds

Textmetadata
LicenceTDM
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.