Evidence map›Paper›PMID 30774309›Full record

ArticleDrug design, development and therapy2019

Structure-activity relationship of an antimicrobial peptide, Phylloseptin-PHa: balance of hydrophobicity and charge determines the selectivity of bioactivities.

Yuzhang Liu, Qiang Du, Chengbang Ma, Xinping Xi, Lei Wang, Mei Zhou, James F Burrows, Tianbao Chen, Hui Wang

Open access · goldAbstract read
In one paragraph

Article in Drug design, development and therapy, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

20 citing papers in PubMed, 40 citations in OpenAlex.

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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 at 2 institutions in 2 countries.

Yuzhang LiuSchool of Pharmacy, China Medical University, Shenyang 110001, Liaoning, China, hwang@cmu.edu.cn.
Qiang DuSchool of Pharmacy, China Medical University, Shenyang 110001, Liaoning, China, hwang@cmu.edu.cn.
Chengbang MaFaculty of Medicine, Health and Life Sciences, School of Pharmacy, Queen's University Belfast, Belfast BT9 7BL, Northern Ireland, UK, c.ma@qub.ac.uk.
Xinping XiFaculty of Medicine, Health and Life Sciences, School of Pharmacy, Queen's University Belfast, Belfast BT9 7BL, Northern Ireland, UK, c.ma@qub.ac.uk.
Lei WangFaculty of Medicine, Health and Life Sciences, School of Pharmacy, Queen's University Belfast, Belfast BT9 7BL, Northern Ireland, UK, c.ma@qub.ac.uk.
Mei ZhouFaculty of Medicine, Health and Life Sciences, School of Pharmacy, Queen's University Belfast, Belfast BT9 7BL, Northern Ireland, UK, c.ma@qub.ac.uk.
James F BurrowsFaculty of Medicine, Health and Life Sciences, School of Pharmacy, Queen's University Belfast, Belfast BT9 7BL, Northern Ireland, UK, c.ma@qub.ac.uk.
Tianbao ChenFaculty of Medicine, Health and Life Sciences, School of Pharmacy, Queen's University Belfast, Belfast BT9 7BL, Northern Ireland, UK, c.ma@qub.ac.uk.
Hui WangSchool of Pharmacy, China Medical University, Shenyang 110001, Liaoning, China, hwang@cmu.edu.cn.
Queen's University Belfast · GBChina Medical University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundAntimicrobial peptides (AMPs) from the skin secretions of amphibians are now considered as a potential alternative to conventional antibiotics. Phylloseptins are a family of AMPs identified in the skin secretions of Phyllomedusinae tree frogs which exhibit highly conserved structural characteristics. This study examines the structure-activity relationship of the newly discovered phylloseptin, Phylloseptin-PHa (PSPHa) from MATERIALS AND

methodsPSPHa and modified analogs were produced by solid phase synthesis and purified by reverse-phase HPLC. Rationally designed modified analogs incorporating changes in significant physicochemical parameters such as hydrophobicity, hydrophobic moment and net charge were investigated to determine their influence on secondary structure, antimicrobial activity, membrane permeabilization and cytotoxicity.

resultsOverall, we found that when rationally designing AMPs by altering their primary structure it is important to keep a balance between hydrophobicity and charge.

conclusionThis study provides new insights which will help in the future development of AMPs as alternatives to conventional antibiotics for the treatment of

Indexed as

Anti-Bacterial AgentsAntimicrobial Cationic PeptidesChromatography, High Pressure LiquidHydrophobic and Hydrophilic InteractionsMicrobial Sensitivity TestsSolid-Phase Synthesis TechniquesStaphylococcal InfectionsStaphylococcus aureusStructure-Activity RelationshipAnti-Bacterial AgentsAntimicrobial Cationic Peptidesantimicrobial activitychargehydrophobicitymembrane selectivityphylloseptin

Identifiers

PMID30774309
PMCPMC6350648
OpenAlexW2914649046

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.