Evidence map›Paper›PMID 27588549›Full record

ArticleACS chemical biology2016

Thermal Unthreading of the Lasso Peptides Astexin-2 and Astexin-3.

Caitlin D Allen, Maria Y Chen, Alexander Y Trick, Dan Thanh Le, Andrew L Ferguson, A James Link

Abstract read
In one paragraph

Article in ACS chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
3.9field-weighted citation impact, top 7% 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

33 citing papers in PubMed, 57 citations in OpenAlex.

  1. Tangled Tail of Mechanically Interlocked Peptides.Journal of the American Chemical Society · 2026
    Review
  2. Article
  3. Lasso Peptides-A New Weapon Against Superbugs.International journal of molecular sciences · 2025
    Review
  4. Article
  5. Article
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  15. Article
  16. Review
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  19. How to harness biosynthetic gene clusters of lasso peptides.Journal of industrial microbiology & biotechnology · 2020
    Review
  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

6 authors at 2 institutions in 1 country.

Caitlin D AllenDepartments of Chemical and Biological Engineering and ‡Molecular Biology, Princeton University , Princeton, New Jersey 08544, United States.
Maria Y ChenDepartments of Chemical and Biological Engineering and ‡Molecular Biology, Princeton University , Princeton, New Jersey 08544, United States.
Alexander Y TrickDepartments of Chemical and Biological Engineering and ‡Molecular Biology, Princeton University , Princeton, New Jersey 08544, United States.
Dan Thanh LeDepartments of Chemical and Biological Engineering and ‡Molecular Biology, Princeton University , Princeton, New Jersey 08544, United States.
Andrew L FergusonDepartments of Chemical and Biological Engineering and ‡Molecular Biology, Princeton University , Princeton, New Jersey 08544, United States.
A James LinkDepartments of Chemical and Biological Engineering and ‡Molecular Biology, Princeton University , Princeton, New Jersey 08544, United States.
University of Illinois Urbana-Champaign · USPrinceton University · US

Funding

Lasso Peptide DiscoveryR01GM107036 · NIGMS · PRINCETON UNIVERSITY · PI LINK, AARON JAMES · 2014 to 2022
$2.9M
NIGMS NIH HHS R01 GM107036
6 · The paper itself

Abstract

Lasso peptides are a class of knot-like polypeptides in which the C-terminal tail of the peptide threads through a ring formed by an isopeptide bond between the N-terminal amine group and a side chain carboxylic acid. The small size (∼20 amino acids) and simple topology of lasso peptides make them a good model system for studying the unthreading of entangled polypeptides, both with experiments and atomistic simulation. Here, we present an in-depth study of the thermal unthreading behavior of two lasso peptides astexin-2 and astexin-3. Quantitative kinetics and energetics of the unthreading process were determined for variants of these peptides using a series of chromatography and mass spectrometry experiments and biased molecular dynamics (MD) simulations. In addition, we show that the Tyr15Phe variant of astexin-3 unthreads via an unprecedented "tail pulling" mechanism. MD simulations on a model ring-thread system coupled with machine learning approaches also led to the discovery of physicochemical descriptors most important for peptide unthreading.

Indexed as

KineticsMolecular Dynamics SimulationPeptidesProtein StabilityPeptides

Identifiers

PMID27588549
PMCPMC5148663
OpenAlexW2516895464

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.