Evidence map›Paper›PMID 35931667›Full record

ArticleNature communications2022

Multifunctional synthetic nano-chaperone for peptide folding and intracellular delivery.

Il-Soo Park, Seongchan Kim, Yeajee Yim, Ginam Park, Jinahn Choi, Cheolhee Won, Dal-Hee Min

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.7field-weighted citation impact, top 14% 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

10 citing papers in PubMed, 17 citations in OpenAlex.

  1. Induction and Stabilization of Peptide Alpha-Helices on Silica Nanoparticles.Angewandte Chemie (International ed. in English) · 2026
    Article
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  5. Review
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  10. Strategies for Improving Peptide Stability and Delivery.Pharmaceuticals (Basel, Switzerland) · 2022
    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

7 authors at 4 institutions in 2 countries.

Il-Soo Park *Department of Chemistry, Seoul National University, Seoul, 08826, Republic of Korea.
Seongchan Kim *Biomaterials Research Center, Biomedical Research Division, Korea Institute of Science and Technology (KIST), Seoul, 02792, Republic of Korea.
Yeajee YimDepartment of Chemistry, Seoul National University, Seoul, 08826, Republic of Korea.ORCID 0000-0002-1762-8668
Ginam ParkDepartment of Chemistry, Seoul National University, Seoul, 08826, Republic of Korea.
Jinahn ChoiDepartment of Chemistry, Seoul National University, Seoul, 08826, Republic of Korea.
Cheolhee WonInstitute of Biotherapeutics Convergence Technology, Lemonex Inc, Seoul, 06683, Republic of Korea.
Dal-Hee MinDepartment of Chemistry, Seoul National University, Seoul, 08826, Republic of Korea. dalheemin@snu.ac.kr.ORCID 0000-0001-8623-6716
Seoul National University · KRAdvanced Institute of Convergence Technology · KRKorea Institute of Science and Technology · KRLemonex (South Korea) · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Artificial, synthetic chaperones have attracted much attention in biomedical research due to their ability to control the folding of proteins and peptides. Here, we report bio-inspired multifunctional porous nanoparticles to modulate proper folding and intracellular delivery of therapeutic α-helical peptide. The Synthetic Nano-Chaperone for Peptide (SNCP) based on porous nanoparticles provides an internal hydrophobic environment which contributes in stabilizing secondary structure of encapsulated α-helical peptides due to the hydrophobic internal environments. In addition, SNCP with optimized inner surface modification not only improves thermal stability for α-helical peptide but also supports the peptide stapling methods in situ, serving as a nanoreactor. Then, SNCP subsequently delivers the stabilized therapeutic α-helical peptides into cancer cells, resulting in high therapeutic efficacy. SNCP improves cellular uptake and bioavailability of the anti-cancer peptide, so the cancer growth is effectively inhibited in vivo. These data indicate that the bio-inspired SNCP system combining nanoreactor and delivery carrier could provide a strategy to expedite the development of peptide therapeutics by overcoming existing drawbacks of α-helical peptides as drug candidates.

Indexed as

Molecular ChaperonesPeptidesAmino Acid SequenceProtein Conformation, alpha-HelicalProtein FoldingProtein Structure, SecondaryMolecular ChaperonesPeptides

Identifiers

PMID35931667
PMCPMC9356039
OpenAlexW4289944373

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.