Evidence map›Paper›PMID 38419760›Full record

ArticleAsian journal of pharmaceutical sciences2024

Design of pH-responsive antimicrobial peptide melittin analog-camptothecin conjugates for tumor therapy.

Sujie Huang, Yuxuan Gao, Ling Ma, Bo Jia, Wenhao Zhao, Yufan Yao, Wenyuan Li, Tongyi Lin, Rui Wang, Jingjing Song and 1 more

Open access · diamondAbstract read
In one paragraph

Article in Asian journal of pharmaceutical sciences, 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
4.0field-weighted citation impact, top 7% 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, 9 citations in OpenAlex.

  1. Review
  2. Review
  3. 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

11 authors at 2 institutions in 1 country.

Sujie HuangInstitute of Pharmacology, School of Basic Medical Sciences, Lanzhou University, Lanzhou 730000, China.
Yuxuan GaoInstitute of Pharmacology, School of Basic Medical Sciences, Lanzhou University, Lanzhou 730000, China.
Ling MaInstitute of Pharmacology, School of Basic Medical Sciences, Lanzhou University, Lanzhou 730000, China.
Bo JiaKey Laboratory of Preclinical Study for New Drugs of Gansu Province, School of Basic Medical Sciences & Research Unit of Peptide Science, Chinese Academy of Medical Sciences, Lanzhou University, Lanzhou 730000, China.
Wenhao ZhaoLanzhou University Second Hospital, Lanzhou University, Lanzhou 730000, China.
Yufan YaoKey Laboratory of Preclinical Study for New Drugs of Gansu Province, School of Basic Medical Sciences & Research Unit of Peptide Science, Chinese Academy of Medical Sciences, Lanzhou University, Lanzhou 730000, China.
Wenyuan LiKey Laboratory of Preclinical Study for New Drugs of Gansu Province, School of Basic Medical Sciences & Research Unit of Peptide Science, Chinese Academy of Medical Sciences, Lanzhou University, Lanzhou 730000, China.
Tongyi LinLanzhou University Second Hospital, Lanzhou University, Lanzhou 730000, China.
Rui WangKey Laboratory of Preclinical Study for New Drugs of Gansu Province, School of Basic Medical Sciences & Research Unit of Peptide Science, Chinese Academy of Medical Sciences, Lanzhou University, Lanzhou 730000, China.
Jingjing SongInstitute of Pharmacology, School of Basic Medical Sciences, Lanzhou University, Lanzhou 730000, China.
Wei ZhangKey Laboratory of Preclinical Study for New Drugs of Gansu Province, School of Basic Medical Sciences & Research Unit of Peptide Science, Chinese Academy of Medical Sciences, Lanzhou University, Lanzhou 730000, China.
Chinese Academy of Medical Sciences & Peking Union Medical College · CNLanzhou University Second Hospital · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Melittin, a classical antimicrobial peptide, is a highly potent antitumor agent. However, its significant toxicity seriously hampers its application in tumor therapy. In this study, we developed novel melittin analogs with pH-responsive, cell-penetrating and membrane-lytic activities by replacing arginine and lysine with histidine. After conjugation with camptothecin (CPT), CPT-AAM-1 and CPT-AAM-2 were capable of killing tumor cells by releasing CPT at low concentrations and disrupting cell membranes at high concentrations under acidic conditions. Notably, we found that the C-terminus of the melittin analogs was more suitable for drug conjugation than the N-terminus. CPT-AAM-1 significantly suppressed melanoma growth

Indexed as

Antimicrobial peptideAntitumor activityCell-penetrating activityMembrane disruptionPeptide-drug conjugate

Identifiers

PMID38419760
PMCPMC10900806
OpenAlexW4391824613

What OpenQuestion holds

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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.