Evidence map›Paper›PMID 27276534›Full record

ArticleAngewandte Chemie (International ed. in English)2016

Short Self-Assembling Peptides Are Able to Bind to Copper and Activate Oxygen.

Olga V Makhlynets, Pallavi M Gosavi, Ivan V Korendovych

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
6.2field-weighted citation impact, top 3% 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

41 citing papers in PubMed, 137 citations in OpenAlex.

  1. Article
  2. Catalytic Amyloids: Turning Fibrils Into Biocatalysts.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026
    Review
  3. Structure-activity relationships in catalytic amyloids.Journal of inorganic biochemistry · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Catalysis driven by an amyloid-substrate complex.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. Article
  10. Article
  11. Autohydrolysis of Diglycine-Activated Succinic Esters Boosts Cellular Uptake.Angewandte Chemie (International ed. in English) · 2023
    Article
  12. Article
  13. Article
  14. Review
  15. Catalytically Active Amyloids as Future Bionanomaterials.Nanomaterials (Basel, Switzerland) · 2022
    Review
  16. Review
  17. Catalysis and Electron Transfer inChemical reviews · 2022
    Review
  18. Nanoscale · 2022
    Article
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

Olga V MakhlynetsDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA.
Pallavi M GosaviDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA.
Ivan V KorendovychDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA. ikorendo@syr.edu.ORCID 0000-0001-8144-783X
Syracuse University · US

Funding

TR&D 4 for ACERT, 2017-2021 funding periodP41GM103521 · NIGMS · CORNELL UNIVERSITY · PI FREED, JACK H · 2012 to 2021
$11.7M
Understanding Evolution of Protein Function Through Design.R35GM119634 · NIGMS · SYRACUSE UNIVERSITY · PI KORENDOVYCH, IVAN V · 2016 to 2025
$4.3M
NIGMS NIH HHS P41 GM103521NIGMS NIH HHS R35 GM119634
6 · The paper itself

Abstract

We have shown that de novo designed peptides self-assemble in the presence of copper to create supramolecular assemblies capable of carrying out the oxidation of dimethoxyphenol in the presence of dioxygen. Formation of the supramolecular assembly, which is akin to a protein fold, is critical for productive catalysis since peptides possessing the same functional groups but lacking the ability to self-assemble do not catalyze substrate oxidation. The ease with which we have discovered robust and productive oxygen activation catalysts suggests that these prion-like assemblies might have served as intermediates in the evolution of enzymatic function and opens the path for the development of new catalyst nanomaterials.

Indexed as

Binding SitesCatalysisCopperOxygenPeptidesCopperOxygenPeptidescatalysiscopperpeptidesself-assemblysupramolecular chemistry

Identifiers

PMID27276534
PMCPMC5064842
OpenAlexW2416087370

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.