Evidence map›Paper›PMID 38124427›Full record

ArticleJournal of medicinal chemistry2024

Proline-Hinged α-Helical Peptides Sensitize Gram-Positive Antibiotics, Expanding Their Physicochemical Properties to Be Used as Gram-Negative Antibiotics.

Yoonhwa Choi, Hyeong Woon Choe, Minsoo Kook, Seolah Choo, Tae Woo Park, Soeun Bae, Heeseung Kim, Jihye Yang, Woo-Seong Jeong, Jiyoung Yu and 3 more

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of medicinal chemistry, 2024. 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
1.5field-weighted citation impact, top 18% 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

3 citing papers in PubMed, 8 citations in OpenAlex.

  1. Anti-Antibiotics (Basel, Switzerland) · 2025
    Article
  2. Review
  3. Proline-Modified (RW)ACS omega · 2025
    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

13 authors at 3 institutions in 2 countries.

Yoonhwa ChoiDepartment of Chemistry & Education, Seoul National University, Seoul 08826, Republic of Korea.
Hyeong Woon ChoeDepartment of Chemistry & Education, Seoul National University, Seoul 08826, Republic of Korea.
Minsoo KookDepartment of Infectious Disease, Asan Medical Center, University of Ulsan College of Medicine, Seoul 05505, Republic of Korea.
Seolah ChooDepartment of Chemistry & Education, Seoul National University, Seoul 08826, Republic of Korea.
Tae Woo ParkDepartment of Chemistry & Education, Seoul National University, Seoul 08826, Republic of Korea.
Soeun BaeDepartment of Chemistry & Education, Seoul National University, Seoul 08826, Republic of Korea.
Heeseung KimDepartment of Infectious Disease, Asan Medical Center, University of Ulsan College of Medicine, Seoul 05505, Republic of Korea.
Jihye YangDepartment of Infectious Disease, Asan Medical Center, University of Ulsan College of Medicine, Seoul 05505, Republic of Korea.
Woo-Seong JeongLaboratory Animal Resource Center, Korea Research Institute of Bioscience and Biotechnology, Cheongju 28116, Republic of Korea.
Jiyoung YuAsan Medical Center, Seoul 05505, Republic of Korea.
Kyeong-Ryoon LeeLaboratory Animal Resource Center, Korea Research Institute of Bioscience and Biotechnology, Cheongju 28116, Republic of Korea.ORCID 0000-0003-2175-8876
Yang Soo KimDepartment of Infectious Disease, Asan Medical Center, University of Ulsan College of Medicine, Seoul 05505, Republic of Korea.
Jaehoon YuDepartment of Chemistry & Education, Seoul National University, Seoul 08826, Republic of Korea.ORCID 0000-0003-4222-4398
Seoul National University of Education · KRUlsan College · KRKorea Research Institute of Bioscience and Biotechnology · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The outer membrane (OM) of Gram-negative bacteria is the most difficult obstacle for small-molecule antibiotics to reach their targets in the cytosol. The molecular features of Gram-negative antibiotics required for passing through the OM are that they should be positively charged rather than neutral, flat rather than globular, less flexible, or more increased amphiphilic moment. Because of these specific molecular characteristics, developing Gram-negative antibiotics is difficult. We focused on sensitizer peptides to facilitate the passage of hydrophobic Gram-positive antibiotics through the OM. We explored ways of improving the sensitizing ability of proline-hinged α-helical peptides by adjusting their length, hydrophobicity, and N-terminal groups. A novel peptide, 1403, improves the potentiation of rifampicin

Indexed as

Anti-Bacterial AgentsProlineGram-Negative BacteriaMicrobial Sensitivity TestsPeptidesRifampinAnti-Bacterial AgentsPeptidesProlineRifampin

Identifiers

PMID38124427
PMCPMC10860147
OpenAlexW4390061282

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.