Evidence map›Paper›PMID 41145472›Full record

ArticleNature communications2025

Assembly of dynamic helical β-peptides with switchable handedness into multiple types of metal-peptide frameworks.

Ingyu Han, Ha-Jin Lee, Ilia A Guzei, Soo Hyuk Choi

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

4 authors.

Ingyu HanDepartment of Chemistry, Yonsei University, Seoul, Republic of Korea.ORCID http://orcid.org/0009-0000-7395-1286
Ha-Jin LeeDivision of Chemistry and Bio-Environmental Sciences, Seoul Women's University, Seoul, Republic of Korea.
Ilia A GuzeiDepartment of Chemistry, University of Wisconsin, Madison, WI, USA.ORCID http://orcid.org/0000-0003-1976-7386
Soo Hyuk ChoiDepartment of Chemistry, Yonsei University, Seoul, Republic of Korea. sh-choi@yonsei.ac.kr.ORCID http://orcid.org/0000-0003-4066-6504

Funding

Korea Health Industry Development Institute (KHIDI) HI22C2004National Research Foundation of Korea (NRF) NRF-2021R1A2C1013477National Research Foundation of Korea (NRF) RS-2024-00401422
6 · The paper itself

Abstract

Metal-directed assemblies of helical peptides are emerging chiral biomimetic materials, yet dynamic helical peptides remain underexplored. Here we report the coordination-driven assembly of dynamic 12/10-helical β-pentapeptides into distinct metal-peptide frameworks (MPFs) with silver ions. Ligand 1, consisting of cis-2-aminocycloheptanecarboxylic acid with alternating chirality, exhibits solvent-dependent screw-sense preference: (P)-helix in protic and (M)-helix in aprotic solvents. The two helical conformers are not enantiomers and assemble into two distinct MPFs (Ag-1M and Ag-1P), while a racemic ligand mixture (1 and ent-1) yields a third MPF (Ag-rac-1PM). A series of modified ligands (2-5), incorporating various central residues, form MPFs analogous to Ag-1M or Ag-1P, with pore environments modulated by side chains. Particularly, an MPF incorporating polar N-acetyl azepane moieties (Ag-5M) selectively recognizes a chiral guest through post-crystallization. These results highlight dynamic helical β-peptides as versatile building blocks for diverse chiral MPFs, with tunable pore environments through rational peptide design.

Indexed as

PeptidesSilverLigandsModels, MolecularProtein Structure, SecondaryStereoisomerismLigandsPeptidesSilver

Identifiers

PMID41145472
PMCPMC12559420

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.