Evidence map›Paper›PMID 35442694›Full record

ArticleOrganic letters2022

Optimizing the Local Chemical Environment on a Bifunctional Helical Peptide Scaffold Enables Enhanced Enantioselectivity and Cooperative Catalysis.

Adam X Wayment, Mariur Rodriguez Moreno, Carter J Jones, Gabriel J Smith, Parker Jarman, Nayeli J Garcia Morin, Morgan J Coombs, Jacob A Parkman, Connor D Barlow, Stacy Allington Smith and 2 more

Abstract read
In one paragraph

Article in Organic letters, 2022. 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. Article
  2. Article
  3. 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

12 authors.

Adam X WaymentDepartment of Chemistry and Biochemistry, Brigham Young University, Provo, Utah 84602, United States.
Mariur Rodriguez MorenoDepartment of Chemistry and Biochemistry, Brigham Young University, Provo, Utah 84602, United States.
Carter J JonesDepartment of Chemistry and Biochemistry, Brigham Young University, Provo, Utah 84602, United States.
Gabriel J SmithDepartment of Chemistry and Biochemistry, Brigham Young University, Provo, Utah 84602, United States.
Parker JarmanDepartment of Chemistry and Biochemistry, Brigham Young University, Provo, Utah 84602, United States.
Nayeli J Garcia MorinDepartment of Chemistry and Biochemistry, Brigham Young University, Provo, Utah 84602, United States.
Morgan J CoombsDepartment of Chemistry and Biochemistry, Brigham Young University, Provo, Utah 84602, United States.
Jacob A ParkmanDepartment of Chemistry and Biochemistry, Brigham Young University, Provo, Utah 84602, United States.
Connor D BarlowDepartment of Chemistry and Biochemistry, Brigham Young University, Provo, Utah 84602, United States.
Stacy Allington SmithDepartment of Chemistry and Biochemistry, Brigham Young University, Provo, Utah 84602, United States.
Scott R BurtDepartment of Chemistry and Biochemistry, Brigham Young University, Provo, Utah 84602, United States.
David J MichaelisDepartment of Chemistry and Biochemistry, Brigham Young University, Provo, Utah 84602, United States.ORCID 0000-0003-3914-5752

Funding

Multifunctional enzyme-like catalysts for organic synthesisR15GM134476 · NIGMS · BRIGHAM YOUNG UNIVERSITY · PI MICHAELIS, DAVID JOHN · 2019 to 2019
$437k
NIGMS NIH HHS R15 GM134476
6 · The paper itself

Abstract

We describe a proof-of-concept study in which peptide-bound enamine and thiourea catalysts are used to facilitate the conjugate addition of cyclohexanone to nitroolefins. Our bifunctional peptide scaffold is modified to optimize the local environment around both catalysts to enhance both reactivity and enantioselectivity, affording selectivities of ≤95% ee. Circular dichroism, nuclear magnetic resonance nuclear Overhauser effect studies, and molecular dynamics simulations verify the helical structure of our catalyst in solution and the importance of the secondary structure in catalysis.

Indexed as

PeptidesThioureaCatalysisMolecular StructureStereoisomerismPeptidesThiourea

Identifiers

PMID35442694
PMCPMC9248067

What OpenQuestion holds

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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.