Evidence map›Paper›PMID 32956537›Full record

ArticleChembiochem : a European journal of chemical biology2021

Covalent Linkage and Macrocylization Preserve and Enhance Synergistic Interactions in Catalytic Amyloids.

Zsofia Lengyel-Zhand, Liam R Marshall, Maximilian Jung, Megha Jayachandran, Min-Chul Kim, Austin Kriews, Olga V Makhlynets, H Christopher Fry, Armin Geyer, Ivan V Korendovych

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Structure-activity relationships in catalytic amyloids.Journal of inorganic biochemistry · 2026
    Article
  2. Article
  3. 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

10 authors.

Zsofia Lengyel-ZhandDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, NY 13244, USA.
Liam R MarshallDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, NY 13244, USA.
Maximilian JungDepartment of Chemistry, Philipps-Universität Marburg, Hans-Meerwein-Straße 4, 35032, Marburg, Germany.
Megha JayachandranDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, NY 13244, USA.
Min-Chul KimDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, NY 13244, USA.
Austin KriewsDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, NY 13244, USA.
Olga V MakhlynetsDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, NY 13244, USA.
H Christopher FryCenter for Nanoscale Materials, Argonne National Laboratory, Lemont, IL 60439, USA.
Armin GeyerDepartment of Chemistry, Philipps-Universität Marburg, Hans-Meerwein-Straße 4, 35032, Marburg, Germany.
Ivan V KorendovychDepartment of Chemistry, Syracuse University, 111 College Place, Syracuse, NY 13244, USA.ORCID 0000-0001-8144-783X

Funding

Understanding Evolution of Protein Function Through Design.R35GM119634 · NIGMS · SYRACUSE UNIVERSITY · PI KORENDOVYCH, IVAN V · 2016 to 2025
$4.3M
NIGMS NIH HHS R35 GM119634
6 · The paper itself

Abstract

The self-assembly of short peptides into catalytic amyloid-like nanomaterials has proven to be a powerful tool in both understanding the evolution of early proteins and identifying new catalysts for practically useful chemical reactions. Here we demonstrate that both parallel and antiparallel arrangements of β-sheets can accommodate metal ions in catalytically productive coordination environments. Moreover, synergistic relationships, identified in catalytic amyloid mixtures, can be captured in macrocyclic and sheet-loop-sheet species, that offer faster rates of assembly and provide more complex asymmetric arrangements of functional groups, thus paving the way for future designs of amyloid-like catalytic proteins. Our findings show how initial catalytic activity in amyloid assemblies can be propagated and improved in more-complex molecules, providing another link in a complex evolutionary chain between short, potentially abiotically produced peptides and modern-day enzymes.

Indexed as

AmyloidCatalysisCyclizationOrganometallic CompoundsAmyloidOrganometallic Compoundsamyloidscatalysispeptidesself-assemblysynergistic interactions

Identifiers

PMID32956537
PMCPMC8009494

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.