Evidence map›Paper›PMID 35390261›Full record

ArticleJournal of the American Chemical Society2022

Assembly of π-Stacking Helical Peptides into a Porous and Multivariable Proteomimetic Framework.

Sherrie L Heinz-Kunert, Ashma Pandya, Viet Thuc Dang, Phuong Nguyen Tran, Sabari Ghosh, Dan McElheny, Bernard D Santarsiero, Zhong Ren, Andy I Nguyen

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Article
  2. Nanographene-Based van der Waals Organic Framework With Permanent Porosity.Angewandte Chemie (International ed. in English) · 2026
    Article
  3. Article
  4. Article
  5. Review
  6. Emergent properties of supramolecular peptide assemblies.Chemical communications (Cambridge, England) · 2026
    Review
  7. Article
  8. Discrete Actuation of Water-Responsive Crystalline Metal-Peptide Frameworks.Angewandte Chemie (International ed. in English) · 2025
    Article
  9. Article
  10. Metal-α-Helix Peptide Frameworks.Journal of the American Chemical Society · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors.

Sherrie L Heinz-KunertDepartment of Chemistry, University of Illinois at Chicago, Chicago, Illinois 60607, United States.
Ashma PandyaDepartment of Chemistry, University of Illinois at Chicago, Chicago, Illinois 60607, United States.ORCID 0000-0003-3303-1009
Viet Thuc DangDepartment of Chemistry, University of Illinois at Chicago, Chicago, Illinois 60607, United States.
Phuong Nguyen TranDepartment of Chemistry, University of Illinois at Chicago, Chicago, Illinois 60607, United States.
Sabari GhoshDepartment of Chemistry, University of Illinois at Chicago, Chicago, Illinois 60607, United States.
Dan McElhenyDepartment of Chemistry, University of Illinois at Chicago, Chicago, Illinois 60607, United States.
Bernard D SantarsieroDepartment of Pharmaceutical Sciences, University of Illinois at Chicago, Chicago, Illinois 60607, United States.ORCID 0000-0002-9032-9699
Zhong RenDepartment of Chemistry, University of Illinois at Chicago, Chicago, Illinois 60607, United States.ORCID 0000-0001-7098-3127
Andy I NguyenDepartment of Chemistry, University of Illinois at Chicago, Chicago, Illinois 60607, United States.ORCID 0000-0003-4137-6453

Funding

Structures, Dynamics and Signaling Mechanisms of Modular PhotoreceptorsR01EY024363 · NEI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI YANG, XIAOJING · 2014 to 2021
$2.9M
NEI NIH HHS R01 EY024363
6 · The paper itself

Abstract

The evolution of proteins from simpler, self-assembled peptides provides a powerful blueprint for the design of complex synthetic materials. Previously, peptide-metal frameworks using short sequences (≤3 residues) have shown great promise as proteomimetic materials that exhibit sophisticated capabilities. However, their development has been hindered due to few variable residues and restricted choice of side-chains that are compatible with metal ions. Herein, we developed a noncovalent strategy featuring π-stacking bipyridyl residues to assemble much longer peptides into crystalline frameworks that tolerate even previously incompatible acidic and basic functionalities and allow an unprecedented level of pore variations. Single-crystal X-ray structures are provided for all variants to guide and validate rational design. These materials exhibit hallmark proteomimetic behaviors such as guest-selective induced fit and assembly of multimetallic units. Significantly, we demonstrate facile optimization of the framework design to substantially increase affinity toward a complex organic molecule.

Indexed as

MetalsPeptides2,2'-DipyridylPorosityProteins2,2'-DipyridylMetalsPeptidesProteins

Identifiers

PMID35390261
PMCPMC12129299

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.