Evidence map›Paper›PMID 27165480›Full record

ArticleInterdisciplinary sciences, computational life sciences2016

Molecular Design, Structural Analysis and Antifungal Activity of Derivatives of Peptide CGA-N46.

Rui-Fang Li, Zhi-Fang Lu, Ya-Nan Sun, Shi-Hua Chen, Yan-Jie Yi, Hui-Ru Zhang, Shuo-Ye Yang, Guang-Hai Yu, Liang Huang, Chao-Nan Li

Open access · hybridAbstract read
In one paragraph

Article in Interdisciplinary sciences, computational life sciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

15 citing papers in PubMed, 30 citations in OpenAlex.

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  14. Review
  15. 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

10 authors at 1 institution in 1 country.

Rui-Fang LiCollege of Biological Engineering, Henan University of Technology, Zhengzhou, 450001, China. 1375098398@qq.com.
Zhi-Fang LuCollege of Biological Engineering, Henan University of Technology, Zhengzhou, 450001, China.
Ya-Nan SunCollege of Biological Engineering, Henan University of Technology, Zhengzhou, 450001, China.
Shi-Hua ChenCollege of Biological Engineering, Henan University of Technology, Zhengzhou, 450001, China.
Yan-Jie YiCollege of Biological Engineering, Henan University of Technology, Zhengzhou, 450001, China.
Hui-Ru ZhangCollege of Biological Engineering, Henan University of Technology, Zhengzhou, 450001, China.
Shuo-Ye YangCollege of Biological Engineering, Henan University of Technology, Zhengzhou, 450001, China.
Guang-Hai YuCollege of Biological Engineering, Henan University of Technology, Zhengzhou, 450001, China.
Liang HuangCollege of Biological Engineering, Henan University of Technology, Zhengzhou, 450001, China.
Chao-Nan LiCollege of Biological Engineering, Henan University of Technology, Zhengzhou, 450001, China.
Henan University of Technology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chromogranin A (CGA)-N46, a derived peptide of human chromogranin A, has antifungal activity. To further research the active domain of CGA-N46, a series of derivatives were designed by successively deleting amino acid from both terminus of CGA-N46, and the amino acid sequence of each derivative was analyzed by bioinformatic software. Based on the predicted physicochemical properties of the peptides, including half-life time in mammalian reticulocytes (in vitro), yeast (in vivo) and E. coli (in vivo), instability index, aliphatic index and grand average of hydropathicity (GRAVY), the secondary structure, net charge, the distribution of hydrophobic residues and hydrophilic residues, the final derivatives CGA-N15, CGA-N16, CGA-N12 and CGA-N8 were synthesized by solid-phase peptide synthesis. The results of bioinformatic analysis showed that CGA-N46 and its derivatives were α-helix, neutral or weak positive charge, hydrophilic, and CGA-N12 and CGA-N8 were more stable than the other derivatives. The results of circular dichroism confirmed that CGA-N46 and its derived peptides displayed α-helical structure in an aqueous solution and 30 mM sodium dodecylsulfate, but α-helical contents decreased in hydrophobic lipid vesicles. CGA-N15, CGA-N16, CGA-N12 and CGA-N8 had higher antifungal activities than their mother peptide CGA-N46. Among of the derived peptides, CGA-N12 showed the least hemolytic activity. In conclusion, we have successfully identified the active domain of CGA-N46 with strong antifungal activity and weak hemolytic activity, which provides the possibility to develop a new class of antibiotics.

Indexed as

Amino Acid SequenceAnimalsAntifungal AgentsChromogranin ACircular DichroismHemolysisHumansHydrophobic and Hydrophilic InteractionsPeptidesStructure-Activity RelationshipAntifungal AgentsChromogranin APeptidesAntifungal activityAntifungal peptidesBioinformatic analysisCGA-N46Derived peptideHemolytic activityMolecular designStructural analysis

Identifiers

PMID27165480
PMCPMC4982898
OpenAlexW2377195148

What OpenQuestion holds

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LicenceCC BY
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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.