Evidence map›Paper›PMID 37966427›Full record

ArticleAdvanced healthcare materials2024

A pH-Responsive Virus-Like Particle as a Protein Cage for a Targeted Delivery.

Kwan-Jip Kim, Gijeong Kim, Jin-Ho Bae, Ji-Joon Song, Hak-Sung Kim

Open access · hybridAbstract read
In one paragraph

Article in Advanced healthcare materials, 2024. 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
3.2field-weighted citation impact, top 8% 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, 13 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Review
  6. Review
  7. Colloidal Crystallization of Virus-Like Particles with Polycations.Small (Weinheim an der Bergstrasse, Germany) · 2025
    Article
  8. Review
  9. Article
  10. 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

5 authors at 1 institution in 1 country.

Kwan-Jip KimDepartment of Biological Sciences, Korea Advanced Institute of Science and Technology (KAIST), 291 Daehak-ro, Daejon, 34141, South Korea.
Gijeong KimDepartment of Biological Sciences, Korea Advanced Institute of Science and Technology (KAIST), 291 Daehak-ro, Daejon, 34141, South Korea.
Jin-Ho BaeDepartment of Biological Sciences, Korea Advanced Institute of Science and Technology (KAIST), 291 Daehak-ro, Daejon, 34141, South Korea.
Ji-Joon SongDepartment of Biological Sciences, Korea Advanced Institute of Science and Technology (KAIST), 291 Daehak-ro, Daejon, 34141, South Korea.
Hak-Sung KimDepartment of Biological Sciences, Korea Advanced Institute of Science and Technology (KAIST), 291 Daehak-ro, Daejon, 34141, South Korea.ORCID 0000-0002-4034-1892
Korea Advanced Institute of Science and Technology · KR

Funding

National Research Foundation of Korea 2019K1A3A1A4700071National Research Foundation of Korea NRF-2017M3A9F6029755National Research Foundation of Korea NRF-2018H1A2A1061362National Research Foundation of Korea NRF-2019M3E5D6063903National Research Foundation of Korea NRF-2020R1A2B5B03001517National Research Foundation of Korea NRF-2021R1A2C201421811National Research Foundation of Korea NRF-2021R1A2C3010506
6 · The paper itself

Abstract

A stimuli-responsive protein self-assembly offers promising utility as a protein nanocage for biotechnological and medical applications. Herein, the development of a virus-like particle (VLP) that undergoes a transition between assembly and disassembly under a neutral and acidic pH, respectively, for a targeted delivery is reported. The structure of the bacteriophage P22 coat protein is used for the computational design of coat subunits that self-assemble into a pH-responsive VLP. Subunit designs are generated through iterative computational cycles of histidine substitutions and evaluation of the interaction energies among the subunits under an acidic and neutral pH. The top subunit designs are tested and one that is assembled into a VLP showing the highest pH-dependent structural transition is selected. The cryo-EM structure of the VLP is determined, and the structural basis of a pH-triggered disassembly is delineated. The utility of the designed VLP is exemplified through the targeted delivery of a cytotoxic protein cargo into tumor cells in a pH-dependent manner. These results provide strategies for the development of self-assembling protein architectures with new functionality for diverse applications.

Indexed as

Bacteriophage P22Capsid ProteinsHydrogen-Ion ConcentrationCapsid Proteinscomputational designpH-responsive assemblytargeted deliveryvirus-like particle

Identifiers

PMID37966427
PMCPMC11469083
OpenAlexW4388686382

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.