Evidence map›Paper›PMID 29043494›Full record

ArticleProbiotics and antimicrobial proteins2018

Influence of Proline Substitution on the Bioactivity of Mammalian-Derived Antimicrobial Peptide NK-2.

Jiexi Yan, Xiaolei Liang, Chang Liu, Yuemei Cheng, Lanxia Zhou, Kairong Wang, Li Zhao

Abstract read
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In one paragraph

Article in Probiotics and antimicrobial proteins, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.0field-weighted citation impact, top 16% 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

12 citing papers in PubMed, 24 citations in OpenAlex.

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  12. Arminin 1a-C, a novel antimicrobial peptide from ancient metazoanDrug design, development and therapy · 2018
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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

7 authors at 2 institutions in 1 country.

Jiexi YanThe Key Laboratory, The First Hospital of Lanzhou University, Donggang Road, NO.1, Lanzhou, Gansu, 730000, People's Republic of China.
Xiaolei LiangThe Key Laboratory, The First Hospital of Lanzhou University, Donggang Road, NO.1, Lanzhou, Gansu, 730000, People's Republic of China.
Chang LiuThe Key Laboratory, The First Hospital of Lanzhou University, Donggang Road, NO.1, Lanzhou, Gansu, 730000, People's Republic of China.
Yuemei ChengSecond School of Clinical Medicine, Lanzhou University, Lanzhou, 730000, China.
Lanxia ZhouThe Key Laboratory, The First Hospital of Lanzhou University, Donggang Road, NO.1, Lanzhou, Gansu, 730000, People's Republic of China.
Kairong WangSchool of Basic Medical Sciences, Institute of Biochemistry and Molecular Biology, Lanzhou University, Lanzhou, 730000, China.
Li ZhaoThe Key Laboratory, The First Hospital of Lanzhou University, Donggang Road, NO.1, Lanzhou, Gansu, 730000, People's Republic of China. 240281276@qq.com.
Lanzhou University · CNFirst Hospital of Lanzhou University · CN

Funding

Research Funds of the First Hospital of Lanzhou University NO. ldyyyn2015-02the National Natural Science Foundation of China 81573265the National Natural Science Foundation of China 81601351the Natural Science Foundation of Gansu Province 17JR5RA267
6 · The paper itself

Abstract

Multidrug-resistant bacteria are emerging as a global threat, making the search for alternative compounds urgent. Antimicrobial peptides (AMPs) became a promising hotspot due to their distinct action mechanism and possibility to be used as an alternative or complement to traditional antibiotics. However, gaining a better understanding about the relationship between antimicrobial peptides structure and its bioactivity is crucial for the development of next generation of antimicrobial agents. NK-2, derived from mammalian protein NK-lysin, has potent antitumor and bactericidal abilities. As proline was considered to be an effective α-helix breaker due to its restricted conformation, to better comprehend the effects of proline in the structure-activity relationship of NK-2, we constructed two NK-2 analogs. We examined the biological activities of NK-2 and its proline substitution analogs and analyzed the resulting conformational changes. Our results showed that introducing proline into the primary sequence of NK-2 significantly decreased the antitumor, antibacterial, and cytotoxic effects, as well as DNA binding activity by changing the α-helix content. However, α-helical content was not the only determining factor, the position of proline inserted was also critical. This study will allow for clearer insight into the role of proline in structure and bioactivity of NK-2 and provide a foundation for future studies.

Indexed as

Amino Acid SequenceAnti-Bacterial AgentsAntimicrobial Cationic PeptidesBacteriaCell Line, TumorCell SurvivalHumansMicrobial Sensitivity TestsMolecular Sequence DataPeptidesProlineProteolipidsStructure-Activity RelationshipAnti-Bacterial AgentsAntimicrobial Cationic PeptidesNK-lysinpeptide NK-2PeptidesProlineProteolipidsAntimicrobial peptidesMultidrug-resistanceProline substitutionStructure-activity relationship

Identifiers

PMID29043494
OpenAlexW2766596516

What OpenQuestion holds

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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.