Evidence map›Paper›PMID 27551502›Full record

ArticleCell death discovery2016

Development of a lytic peptide derived from BH3-only proteins.

Q Liu, H Zhao, Y Jiang, M Wu, Y Tian, D Wang, Y Lao, N Xu, Z Li

Abstract read
In one paragraph

Article in Cell death discovery, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
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  8. Article
  9. Iterative optimization yields Mcl-1-targeting stapled peptides with selective cytotoxicity to Mcl-1-dependent cancer cells.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  10. Article
  11. 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

9 authors.

Q LiuSchool of Chemical Biology and Biotechnology, Peking University Shenzhen Graduate School, Shenzhen, China; Shenzhen Key Lab of Tissue Engineering, The Second People's Hospital of Shenzhen, Shenzhen, China.
H ZhaoSchool of Chemical Biology and Biotechnology, Peking University Shenzhen Graduate School , Shenzhen, China.
Y JiangSchool of Chemical Biology and Biotechnology, Peking University Shenzhen Graduate School , Shenzhen, China.
M WuSchool of Pharmacy, Shanghai University of Traditional Chinese Medicine , Shanghai, China.
Y TianSchool of Chemical Biology and Biotechnology, Peking University Shenzhen Graduate School , Shenzhen, China.
D WangShenzhen Key Lab of Tissue Engineering, The Second People's Hospital of Shenzhen , Shenzhen, China.
Y LaoSchool of Pharmacy, Shanghai University of Traditional Chinese Medicine , Shanghai, China.
N XuKey Lab in Healthy Science and Technology, Division of Life Science, Tsinghua University Shenzhen Graduate School , Shenzhen, China.
Z LiSchool of Chemical Biology and Biotechnology, Peking University Shenzhen Graduate School , Shenzhen, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Despite great advances in cancer therapy, drug resistance is a difficult hurdle to overcome that requires development of anticancer agents with novel and effective modes of action. In a number of studies, lytic peptides have shown remarkable ability to eliminate cancer cells through a different way from traditional treatments. Lytic peptides are positively charged, amphiphilic, and are efficient at binding and disrupting the negatively charged cell membrane of cancer cells. In this study, we described the anticancer properties of a lytic peptide that was developed on the basis of the alignment of amphiphilic BH3 peptides. Our results demonstrated that the positive charge and conformation constraint were favourable for efficient cancer cell elimination. Artificial BCL-2 homology 3 peptides (ABH3) exhibited effective anticancer effects against a series of cancer cell lines in vitro and in HeLa human cervical tumour xenografts in vivo. ABH3 induced cell death in an apoptosis-independent manner through the lytic properties of the peptide that caused disruption of cell membrane. Our results showed that charge tuning and conformation constraining in a lytic peptide could be applied to optimise the anticancer activity of lytic peptides. These results also suggest that ABH3 may be a promising beginning for the development of additional lytic peptides as anticancer reagents.

Identifiers

PMID27551502
PMCPMC4979451

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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.