Evidence map›Paper›PMID 32128962›Full record

ArticleAngewandte Chemie (International ed. in English)2020

Semi-Rationally Designed Short Peptides Self-Assemble and Bind Hemin to Promote Cyclopropanation.

Oleksii Zozulia, Ivan V Korendovych

Open access · greenAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

25 citing papers in PubMed, 59 citations in OpenAlex.

  1. Review
  2. Article
  3. Catalytic Amyloids: Turning Fibrils Into Biocatalysts.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026
    Review
  4. Structure-activity relationships in catalytic amyloids.Journal of inorganic biochemistry · 2026
    Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Review
  10. Protocellular Heme and Iron-Sulfur Clusters.Accounts of chemical research · 2024
    Review
  11. Article
  12. Mechanisms and pathology of protein misfolding and aggregation.Nature reviews. Molecular cell biology · 2023
    Review
  13. Article
  14. Article
  15. Catalytically Active Amyloids as Future Bionanomaterials.Nanomaterials (Basel, Switzerland) · 2022
    Review
  16. Nanoscale · 2022
    Article
  17. Article
  18. De novo metalloprotein design.Nature reviews. Chemistry · 2022
    Article
  19. Article
  20. Catalytic amyloids: Is misfolding folding?Current opinion in chemical biology · 2021
    Review
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

2 authors at 1 institution in 1 country.

Oleksii ZozuliaDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA.ORCID 0000-0003-3803-4225
Ivan V KorendovychDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, NY, 13244, USA.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

The self-assembly of short peptides gives rise to versatile nanoassemblies capable of promoting efficient catalysis. We have semi-rationally designed a series of seven-residue peptides that form hemin-binding catalytic amyloids to facilitate enantioselective cyclopropanation with efficiencies that rival those of engineered hemin proteins. These results demonstrate that: 1) Catalytic amyloids can bind complex metallocofactors to promote practically important multisubstrate transformations. 2) Even essentially flat surfaces of amyloid assemblies can impart a substantial degree of enantioselectivity without the need for extensive optimization. 3) The ease of peptide preparation allows for straightforward incorporation of unnatural amino acids and the preparation of peptides made from d-amino acids with complete reversal of enantioselectivity.

Indexed as

Amino AcidsAmino Acid SequenceCatalysisCyclopropanesHeminKineticsNanostructuresPeptidesProtein BindingStereoisomerismStyreneAmino AcidscyclopropaneCyclopropanesHeminPeptidesStyreneamyloidscyclopropanationheminpeptidesself-assembly

Identifiers

PMID32128962
PMCPMC7274867
OpenAlexW3009344748

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.