Evidence map›Paper›PMID 33479615›Full record

ArticleRSC medicinal chemistry2020

Discovery and characterization of a novel peptide inhibitor against influenza neuraminidase.

Jianmei Chen, Shujun Feng, Yurui Xu, Xinyu Huang, Jikang Zhang, Jiao Chen, Xueying An, Yu Zhang, Xinghai Ning

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in RSC medicinal chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed.

  1. Review
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  6. Antiviral Peptides as Anti-Influenza Agents.International journal of molecular sciences · 2022
    Review
  7. Review
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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.

Jianmei ChenDepartment of Biomedical Engineering , Nanjing National Laboratory of Microstructures , College of Engineering and Applied Sciences , Nanjing University , Nanjing , Jiangsu 210093 , China . Email: zhangyu2016@nju.edu.cn ; Email: xning@nju.edu.cn.
Shujun FengDepartment of Biomedical Engineering , Nanjing National Laboratory of Microstructures , College of Engineering and Applied Sciences , Nanjing University , Nanjing , Jiangsu 210093 , China . Email: zhangyu2016@nju.edu.cn ; Email: xning@nju.edu.cn.
Yurui XuDepartment of Biomedical Engineering , Nanjing National Laboratory of Microstructures , College of Engineering and Applied Sciences , Nanjing University , Nanjing , Jiangsu 210093 , China . Email: zhangyu2016@nju.edu.cn ; Email: xning@nju.edu.cn.
Xinyu HuangDepartment of Biomedical Engineering , Nanjing National Laboratory of Microstructures , College of Engineering and Applied Sciences , Nanjing University , Nanjing , Jiangsu 210093 , China . Email: zhangyu2016@nju.edu.cn ; Email: xning@nju.edu.cn.
Jikang ZhangDepartment of Biomedical Engineering , Nanjing National Laboratory of Microstructures , College of Engineering and Applied Sciences , Nanjing University , Nanjing , Jiangsu 210093 , China . Email: zhangyu2016@nju.edu.cn ; Email: xning@nju.edu.cn.
Jiao ChenJiangsu Province Academy of Traditional Chinese Medicine , Nanjing , Jiangsu 210028 , China.
Xueying AnState Key Laboratory of Pharmaceutical Biotechnology , Department of Sports Medicine and Adult Reconstructive Surgery , Nanjing Drum Tower Hospital , The Affiliated Hospital of Nanjing University Medical School , 321 Zhongshan Road , Nanjing 210008 , Jiangsu , PR China.
Yu ZhangDepartment of Biomedical Engineering , Nanjing National Laboratory of Microstructures , College of Engineering and Applied Sciences , Nanjing University , Nanjing , Jiangsu 210093 , China . Email: zhangyu2016@nju.edu.cn ; Email: xning@nju.edu.cn.
Xinghai NingDepartment of Biomedical Engineering , Nanjing National Laboratory of Microstructures , College of Engineering and Applied Sciences , Nanjing University , Nanjing , Jiangsu 210093 , China . Email: zhangyu2016@nju.edu.cn ; Email: xning@nju.edu.cn.ORCID 0000-0003-3453-9656

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Neuraminidase, an abundant glycoprotein on the influenza virus surface, plays crucial roles in virus replication. Targeting neuraminidase could be a splendid way for the prevention of the spread of influenza infections. Herein, we have identified an octapeptide (errKPAQP) from a synthesized peptide library, originating from mimicking the binding pocket of oseltamivir in neuraminidase, as a potent peptide neuraminidase inhibitor. The docking-based virtual studies showed that errKPAQP exhibited a strong binding affinity (a docking score of -20.03) and nanomolar affinity (11 nM) to influenza neuraminidase, and can inhibit neuraminidase activity at a concentration as low as 4.25 μM, leading to effective protection of MDCK cells from influenza virus-induced death and replication. Furthermore, errKPAQP presented low hemolytic activity, minimal cytotoxicity, and good pharmacokinetic characteristics, which are imperative for an anti-influenza drug. Importantly, errKPAQP was capable of reducing influenza virus-induced inflammation, the serious damage to the lung tissues, and mortality rates in infected mice, indicating that it could protect against the lethal challenge of influenza viruses

Identifiers

PMID33479615
PMCPMC7433756

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Registered trials

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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.