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ArticleProbiotics and antimicrobial proteins2022

Isolation and Chemical Characterization of an Alpha-Helical Peptide, Dendrocin-ZM1, Derived from Zataria multiflora Boiss with Potent Antibacterial Activity.

Sima Sadat Seyedjavadi, Mehdi Razzaghi-Abyaneh, Mohammad Javad Nasiri, Ali Hashemi, Hossein Goudarzi, Mehrdad Haghighi, Masoud Dadashi, Mehdi Goudarzi, Hadi Zare-Zardini, Behzad Pourhossein

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Article in Probiotics and antimicrobial proteins, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

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0cells of the map it votes in
7citing papers in PubMed
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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.

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3 · Its place in the literature

Who cites it

7 citing papers in PubMed.

  1. Article
  2. Review
  3. Cliotide U1, a Novel Antimicrobial Peptide Isolated FromBioinformatics and biology insights · 2025
    Article
  4. Review
  5. Article
  6. Review
  7. Immunopotentiating properties of chimeric OprF-OprI-PopB protein againstIranian journal of basic medical sciences · 2022
    Article
4 · The record

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5 · Who and what money

Authors and funding

10 authors.

Sima Sadat SeyedjavadiInfectious Diseases and Tropical Medicine Research Center, Shahid Beheshti University of Medical Sciences, Tehran, Iran.
Mehdi Razzaghi-AbyanehDepartment of Mycology, Pasteur Institute of Iran, Tehran, Iran.
Mohammad Javad NasiriInfectious Diseases and Tropical Medicine Research Center, Shahid Beheshti University of Medical Sciences, Tehran, Iran.
Ali HashemiInfectious Diseases and Tropical Medicine Research Center, Shahid Beheshti University of Medical Sciences, Tehran, Iran.
Hossein GoudarziInfectious Diseases and Tropical Medicine Research Center, Shahid Beheshti University of Medical Sciences, Tehran, Iran.
Mehrdad HaghighiDepartment of Infectious Diseases, Imam Hossein Teaching and Medical Hospital, Shahid Beheshti University of Medical Sciences, Tehran, Iran.
Masoud DadashiDepartment of Microbiology, School of Medicine, Alborz University of Medical Sciences, Karaj, Iran.
Mehdi GoudarziInfectious Diseases and Tropical Medicine Research Center, Shahid Beheshti University of Medical Sciences, Tehran, Iran. gudarzim@yahoo.com.
Hadi Zare-ZardiniHematology and Oncology Research Center, Shahid Sadoughi University of Medical Sciences, Yazd, Iran.
Behzad PourhosseinDepartment of Medical Virology, Faculty of Medicine, Hamadan University of Medical Sciences, Hamadan, Iran.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Today, resistance of microorganisms to antibiotics has become a major challenge. To overcome this problem, development of new drugs, besides research on their antibacterial activity, is essential. Among chemical components, antimicrobial peptides (AMPs) exhibit antibacterial activity and can be selected as suitable antimicrobial candidates. In this study, a novel antimicrobial peptide, called dendrocin-ZM1, with a molecular weight of ~3716.48 Da, was isolated from Zataria multiflora Boiss (ZM) and purified via precipitation with ammonium sulfate and reverse-phase HPLC chromatography; it was then sequenced via Edman degradation. The in silico method was used to examine the physicochemical properties of dendrocin-ZM1. In this study, four reference strains (gram-positive and gram-negative) and one clinical vancomycin-resistant Staphylococcus aureus strain were used to survey the antimicrobial activities. Moreover, to examine cytotoxicity and hemolytic activity, a HEK-293 cell line and human red blood cells (RBCs) were used, respectively. Evaluation of the physicochemical properties of dendrocin-ZM1, as an AMP, indicated a net charge of + 7 and a hydrophobicity percentage of 54%. This peptide had an amphipathic alpha-helical conformation. It exhibited broad-spectrum antibacterial activities against the tested strains at minimum inhibitory concentrations (MICs) of 4-16 μg/mL. Besides, this peptide showed negligible hemolysis and cytotoxicity in the MIC range. It also exhibited heat stability at temperatures of 20 to 80 °C and was active in a broad pH range (from 6.0 to 10.0). Overall, the present results suggested dendrocin-ZM1 as a remarkable antimicrobial candidate.

Indexed as

Anti-Infective AgentsMethicillin-Resistant Staphylococcus aureusAnti-Bacterial AgentsHEK293 CellsHemolysisHumansMicrobial Sensitivity TestsPeptidesAnti-Bacterial AgentsAnti-Infective AgentsPeptidesAntimicrobial peptideCytotoxicityEscherichia coliStaphylococcus aureusZataria multiflora

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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.