Evidence map›Paper›PMID 26189239›Full record

ArticleHua xi kou qiang yi xue za zhi = Huaxi kouqiang yixue zazhi = West China journal of stomatology2015

[Differential proteomics on synthetic antimicrobial decapeptide against Streptococcus mutans].

Liu Yi, Fei Wei, Wang Yanjun, Mu Yandong, Wu Hongkun

Open access · greenAbstract read
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Article in Hua xi kou qiang yi xue za zhi = Huaxi kouqiang yixue zazhi = West China journal of stomatology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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1 · What the graph read from it

What it found

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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

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3 · Its place in the literature

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0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

4 · The record

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5 · Who and what money

Authors and funding

5 authors.

Liu Yi
Fei Wei
Wang Yanjun
Mu Yandong
Wu Hongkun

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

objectiveTo compare the protein profiles between decapeptide-treated and untreated planktonic cells of Streptococcus mutans (S. mutans) by differential proteomic analysis to determine and identify the key proteins.

methodsIn our previous study, we investigated decapeptide (KKVVFKVKFK-NH2), which was a novel adenosine monophosphate. Compared with other oral pathogens tested, decapeptide had a preferential antibacterial activity against S. mutans. It also inhibited S. mutans biofilm formation and reduced the one-day developed biofilm. In the present study, we first synthesized decapeptide, and then compared the protein profiles between decapeptide-treated and untreated planktonic cells of S. mutans by two-dimensional gel electrophoresis and matrix-assisted laser desorption ionization time-of-flight mass spectrometry. We also verified different expressions of key protein enolase in the protein level.

resultsThe results showed that decapeptide altered the protein expression of planktonic S. mutans. These proteins were functionally involved in carbohydrate degradation by glycolysis, protein folding, conjunction, transport, translation, adenosine triphosphate binding, protein binding, sequence-specific DNA binding, transcription factor activity, and two-component response regulator activity. Western blot results showed that enolase protein expression decreased obviously in decapeptide-treated cells of S. mutans.

conclusionThe protein expression of S. mutans significantly changed after synthetic antimicrobial decapeptide treatment, suggesting that decapeptide may present a preferential effect on oral caries by changing the expression of certain key proteins, such as enolase protein.

Indexed as

ProteomicsAnti-Bacterial AgentsAnti-Infective AgentsBiofilmsDental CariesDepsipeptidesElectrophoresis, Gel, Two-DimensionalOligopeptidesStreptococcus mutansAnti-Bacterial AgentsAnti-Infective AgentsDepsipeptideslysyl-lysyl-valyl-valyl-phenylalanyl-lysyl-valyl-lysyl-phenylalanyl-lysineOligopeptides

Identifiers

PMID26189239
PMCPMC7041002
OpenAlexW996607030

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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.